A major protein fraction of milk obtained from the WHEY.
Globulins are a group of simple proteins, found in blood plasma and other bodily fluids, which are insoluble in water but soluble in saline solutions and are involved in various biological functions such as immune response, transport, and enzyme regulation.
Proteins obtained from foods. They are the main source of the ESSENTIAL AMINO ACIDS.
A nutritional condition produced by a deficiency of proteins in the diet, characterized by adaptive enzyme changes in the liver, increase in amino acid synthetases, and diminution of urea formation, thus conserving nitrogen and reducing its loss in the urine. Growth, immune response, repair, and production of enzymes and hormones are all impaired in severe protein deficiency. Protein deficiency may also arise in the face of adequate protein intake if the protein is of poor quality (i.e., the content of one or more amino acids is inadequate and thus becomes the limiting factor in protein utilization). (From Merck Manual, 16th ed; Harrison's Principles of Internal Medicine, 12th ed, p406)
Protein hydrolysates are defined as complex mixtures of peptides produced by the enzymatic or chemical breakdown of whole proteins, which can vary in their degree of hydrolysis and molecular weight, and are used in various medical and nutritional applications due to their improved digestibility and bioavailability compared to intact proteins.
Proteins which are present in or isolated from SOYBEANS.
An indication of the contribution of a food to the nutrient content of the diet. This value depends on the quantity of a food which is digested and absorbed and the amounts of the essential nutrients (protein, fat, carbohydrate, minerals, vitamins) which it contains. This value can be affected by soil and growing conditions, handling and storage, and processing.
Proteins which are present in or isolated from vegetables or vegetable products used as food. The concept is distinguished from PLANT PROTEINS which refers to non-dietary proteins from plants.
A mixture of related phosphoproteins occurring in milk and cheese. The group is characterized as one of the most nutritive milk proteins, containing all of the common amino acids and rich in the essential ones.
An element with the atomic symbol N, atomic number 7, and atomic weight [14.00643; 14.00728]. Nitrogen exists as a diatomic gas and makes up about 78% of the earth's atmosphere by volume. It is a constituent of proteins and nucleic acids and found in all living cells.
The process of breakdown of food for metabolism and use by the body.
Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.
An annual legume. The SEEDS of this plant are edible and used to produce a variety of SOY FOODS.
A species of the genus MACACA which typically lives near the coast in tidal creeks and mangrove swamps primarily on the islands of the Malay peninsula.
The mass or quantity of heaviness of an individual. It is expressed by units of pounds or kilograms.
Genetically identical individuals developed from brother and sister matings which have been carried out for twenty or more generations or by parent x offspring matings carried out with certain restrictions. This also includes animals with a long history of closed colony breeding.
Works containing information articles on subjects in every field of knowledge, usually arranged in alphabetical order, or a similar work limited to a special field or subject. (From The ALA Glossary of Library and Information Science, 1983)
The major protein constituents of milk are CASEINS and whey proteins such as LACTALBUMIN and LACTOGLOBULINS. IMMUNOGLOBULINS occur in high concentrations in COLOSTRUM and in relatively lower concentrations in milk. (Singleton and Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed, p554)
The major immunoglobulin isotype class in normal human serum. There are several isotype subclasses of IgG, for example, IgG1, IgG2A, and IgG2B.

Difference between mammary epithelial cells from mature virgin and primiparous mice. (1/563)

Mammary epithelial cells from mature virgin mice are similar to those from primiparous mice in several respects. However, there is one known difference. The cells from the mature virgin must traverse the cell cycle in order to become competent to make casein and enzymatically active alpha-lactalbumin in vitro; those from the primiparous animal can make these proteins without first traversing the cycle. In this regard, cells from human placental lactogen- and prolactin-treated mature virgins are, after involution, similar to those from primiparous mice. The developemental block in the cells from the mature virgin, imposed by preventing cell cycle traversal, has been partially delineated. It does not appear to reside at the levels of ultrastructural maturation or the formation of casein messenger RNA. Rather, the lesion is postranscriptional and may be at the level of translation, or posttranslational modification, or both.  (+info)

Molecular characterization of alpha-lactalbumin folding variants that induce apoptosis in tumor cells. (2/563)

This study characterized a protein complex in human milk that induces apoptosis in tumor cells but spares healthy cells. The active fraction was purified from casein by anion exchange chromatography. Unlike other casein components the active fraction was retained by the ion exchanger and eluted after a high salt gradient. The active fraction showed N-terminal amino acid sequence identity with human milk alpha-lactalbumin and mass spectrometry ruled out post-translational modifications. Size exclusion chromatography resolved monomers and oligomers of alpha-lactalbumin that were characterized using UV absorbance, fluorescence, and circular dichroism spectroscopy. The high molecular weight oligomers were kinetically stable against dissociation into monomers and were found to have an essentially retained secondary structure but a less well organized tertiary structure. Comparison with native monomeric and molten globule alpha-lactalbumin showed that the active fraction contains oligomers of alpha-lactalbumin that have undergone a conformational switch toward a molten globule-like state. Oligomerization appears to conserve alpha-lactalbumin in a state with molten globule-like properties at physiological conditions. The results suggest differences in biological properties between folding variants of alpha-lactalbumin.  (+info)

Met-HGF/SF mediates growth arrest and differentiation in T47D breast cancer cells. (3/563)

Hepatocyte growth factor/scatter factor (HGF/SF) is a pluripotent growth factor that exerts mitogenic, motogenic, and morphogenic effects. To elucidate the cellular mechanisms underlying the pluripotent function of this growth factor, T47D human breast cancer cells were transfected with human hgf/sf. The hgf/sf-positive clones exhibited different levels of biologically functional HGF/SF expression and up-regulation of endogenous Met (HGF/SF receptor) expression. In addition, a constitutive phosphorylation of the receptor on tyrosine residues was detected, establishing a Met-HGF/SF autocrine loop. The autocrine activation of Met caused marked inhibition in cell growth accompanied by cell accumulation at G0/G1. These cells underwent terminal cell differentiation as determined by morphological changes, synthesis of milk proteins such as beta-casein and alpha-lactalbumin, and production of lipid vesicles. Our results demonstrate that Met-HGF/SF, an oncogenic signal transduction pathway, is capable of inducing growth arrest and differentiation in certain breast cancer cells and, thus, may have potential as therapeutic and/or prognostic tools in breast cancer treatment.  (+info)

Isolation and identification of three bactericidal domains in the bovine alpha-lactalbumin molecule. (4/563)

Proteolytic digestion of alpha-lactalbumin by pepsin, trypsin and chymotrypsin yielded three polypeptide fragments with bactericidal properties. Two fragments were obtained from the tryptic digestion. One was a pentapeptide with the sequence EQLTK (residues 1-5) and the other, GYGGVSLPEWVCTTF ALCSEK (residues (17-31)S-S(109-114)), was composed of two polypeptide chains held together by a disulfide bridge. Fragmentation of alpha-lactalbumin by chymotrypsin yielded CKDDQNPH ISCDKF (residues (61-68)S-S(75-80)), also a polypeptide composed of two polypeptide chains held together by a disulfide bridge. The three polypeptides were synthesized and found to exert antimicrobial activities. The polypeptides were mostly active against Gram-positive bacteria. Gram-negative bacteria were only poorly susceptible to the bactericidal action of the polypeptides. GYGGVSLPEWVCTTF ALCSEK was most, EQLTK least bactericidal. Replacement of leucine (23) with isoleucine, having a similar chemical structure but higher hydrophobicity, in the sequence GYGGVSLPEWVCTTF ALCSEK significantly reduced the bactericidal capacity of the polypeptide. Digestion of alpha-lactalbumin by pepsin yielded several polypeptide fragments without antibacterial activity. alpha-Lactalbumin in contrast to its polypeptide fragments was not bactericidal against all the bacterial strains tested. Our results suggest a possible antimicrobial function of alpha-lactalbumin after its partial digestion by endopeptidases.  (+info)

Position-independent and copy-number-related expression of a goat bacterial artificial chromosome alpha-lactalbumin gene in transgenic mice. (5/563)

A bacterial artificial chromosome goat insert comprising the alpha-lactalbumin-encoding transcription unit with approximately 150 and 10 kb of 5'- and 3'-flanking sequences, respectively, was micro-injected into mouse eggs. In six out of seven transgenic lines, the level of mammary tissue- and stage-specific expression was position-independent and copy-number-dependent. The exogenous alpha-lactalbumin yield, about 0.8 mg/ml of milk per copy, compared favourably with the alpha-lactalbumin content of mouse and goat milks, about 0.8 and >1 mg/ml, respectively. This suggests that the insert contains most if not all of the cis-acting elements involved in the full and specific expression of the goat alpha-lactalbumin gene and opens up opportunities to use this vector to target expression of foreign genes in the lactating mammary gland of transgenic animals. The transgene was silent in the seventh line for an unknown reason.  (+info)

Guinea-pig milk-protein synthesis. Isolation and characterization of messenger ribonucleic acids from lactating mammary gland and identification of caseins and pre-alpha-lactalbumin as translation products in heterologous cell-free systems. (6/563)

1. The major milk proteins synthesized by the lactating mammary gland of the guinea pig were identified and designated as caseins A, B and C and alpha-lactalbumin, with estimated mol.wts. of 28000, 25500, 20500 and 14500 respectively. 2. Antisera to the total casein fraction and to alpha-lactalbumin were prepared from rabbits. The milk proteins were also iodinated with either 131I or 125I. 3. A poly(A)-rich RNA fraction was isolated from lactating guinea-pig mammary glands. Isolation was by affinity chromatography on oligo(dT)-cellulose. 4. Examination of this RNA fraction by electrophoresis on polyacrylamide gels containing formamide indicated three major species 1, 2 and 3, with estimated wol.wts. of 5.4 X 10(5) and 3.3 X 10(5), and the apparent absence of rRNA species. 5. The poly(A)-rich RNA stimulated protein synthesis in heterologous cell-free systems based on wheat germ, Krebs II ascites-tumour cells, and the latter supplemented with an initiation factor-3 fraction from rabbit reticulocyte ribosomes. 6. Between 80 and 90% of the protein synthesis directed by the mRNA was for milk proteins. 7. Analysis of the proteins immunoprecipitated by the alpha-lactalbumin antiserum showed in the wheat-germ system that the product was a protein with a molecular weight greater than that of alpha-lactalbumin, whereas in the ascites-tumour-cell systems both this protein and alpha-lactalbumin were found. When the larger protein was treated with CNBr and the resulting peptides were examined, it was shown that the extra peptide was at the N-terminus. This and other evidence is adduced for the initial translation product of alpha-lactalbumin being a precursor with an addition of about ten amino acids at the N-terminus. 8. Similar analysis of the casein immlnospecific proteins produced under the direction of mRNA indicated that the products had a molecular weight that was apparently a littel smaller than that of the caseins synthesized in vivo. This was not consistent with higher-molecular weight casein precursors. 9. Possible explanations for the results obtained are discussed, especially in terms of the physiological significance of the pre-alpha-lactalbumin as a secretory protein.  (+info)

Energetics of solvent and ligand-induced conformational changes in alpha-lactalbumin. (7/563)

The energetics of structural changes in the holo and apo forms of a-lactalbumin and the transition between their native and denatured states induced by binding Ca2+ and Na+ have been studied by differential scanning and isothermal titration microcalorimetry and circular dichroism spectroscopy under various solvent conditions. Removal of Ca2+ from the protein enhances its sensitivity to pH and ionic conditions due to noncompensated negative charge-charge interactions at the cation binding site, which significantly reduces its overall stability. At neutral pH and low ionic strength, the native structure of apo-alpha-lactalbumin is stable below 14 C and undergoes a conformational change to a native-like molten globule intermediate at temperatures above 25 degrees C. The denaturation of either holo- or apo-alpha-lactalbumin is a highly cooperative process that is characterized by an enthalpy of similar magnitude when calculated at the same temperature. Measured by direct calorimetric titration, the enthalpy of Ca2+-binding to apo-LA at pH 7.5 is -7.1 kJ mol(-1) at 5.0 degrees C. which is essentially invariant to protonation effects. This small enthalpy effect infers that stabilization of alpha-lactalbumin by Ca2+ is primarily an entropy driven process, presumably arising from electrostatic interactions and the hydration effect. In contrast to the binding of calcium, the interaction of sodium with apo-LA does not produce a noticeable heat effect and is characterized by its ionic nature rather than specific binding to the metal-binding site. Characterization of the conformational stability and ligand binding energetics of alpha-lactalbumin as a function of solvent conditions furnishes significant insight regarding the molecular flexibility and regulatory mechanism mediated by this protein.  (+info)

Trifluoroethanol-induced conformational transitions of proteins: insights gained from the differences between alpha-lactalbumin and ribonuclease A. (8/563)

The trifluoroethanol (TFE)-induced structural changes of two proteins widely used in folding experiments, bovine alpha-lactalbumin, and bovine pancreatic ribonuclease A, have been investigated. The experiments were performed using circular dichroism spectroscopy in the far- and near-UV region to monitor changes in the secondary and tertiary structures, respectively, and dynamic light scattering to measure the hydrodynamic dimensions and the intermolecular interactions of the proteins in different conformational states. Both proteins behave rather differently under the influence of TFE: alpha-lactalbumin exhibits a molten globule state at low TFE concentrations before it reaches the so-called TFE state, whereas ribonuclease A is directly transformed into the TFE state at TFE concentrations above 40% (v/v). The properties of the TFE-induced states are compared with those of equilibrium and kinetic intermediate states known from previous work to rationalize the use of TFE in yielding information about the folding of proteins. Additionally, we report on the properties of TFE/water and TFE/buffer mixtures derived from dynamic light scattering investigations under conditions used in our experiments.  (+info)

Lactalbumin is a protein found in milk, specifically in the whey fraction. It is a globular protein with a molecular weight of around 14,000 daltons and consists of 123 amino acids. Lactalbumin is denatured and coagulates under heat, which makes it useful in cooking and baking as a stabilizer and emulsifier.

In addition to its use as a food ingredient, lactalbumin has also been studied for its potential health benefits. It contains all essential amino acids and is easily digestible, making it a high-quality source of protein. Some research suggests that lactalbumin may have immune-enhancing properties and could potentially be used in the treatment of certain medical conditions. However, more research is needed to confirm these potential benefits.

Globulins are a type of protein found in blood plasma, which is the clear, yellowish fluid that circulates throughout the body inside blood vessels. They are one of the three main types of proteins in blood plasma, along with albumin and fibrinogen. Globulins play important roles in the immune system, helping to defend the body against infection and disease.

Globulins can be further divided into several subcategories based on their size, electrical charge, and other properties. Some of the major types of globulins include:

* Alpha-1 globulins
* Alpha-2 globulins
* Beta globulins
* Gamma globulins

Gamma globulins are also known as immunoglobulins or antibodies, which are proteins produced by the immune system to help fight off infections and diseases. There are five main classes of immunoglobulins: IgA, IgD, IgE, IgG, and IgM. Each class of immunoglobulin has a different function in the body's defense mechanisms.

Abnormal levels of globulins can be indicative of various medical conditions, such as liver disease, kidney disease, or autoimmune disorders. Therefore, measuring the levels of different types of globulins in the blood is often used as a diagnostic tool to help identify and monitor these conditions.

Dietary proteins are sources of protein that come from the foods we eat. Protein is an essential nutrient for the human body, required for various bodily functions such as growth, repair, and immune function. Dietary proteins are broken down into amino acids during digestion, which are then absorbed and used to synthesize new proteins in the body.

Dietary proteins can be classified as complete or incomplete based on their essential amino acid content. Complete proteins contain all nine essential amino acids that cannot be produced by the human body and must be obtained through the diet. Examples of complete protein sources include meat, poultry, fish, eggs, dairy products, soy, and quinoa.

Incomplete proteins lack one or more essential amino acids and are typically found in plant-based foods such as grains, legumes, nuts, and seeds. However, by combining different incomplete protein sources, it is possible to obtain all the essential amino acids needed for a complete protein diet. This concept is known as complementary proteins.

It's important to note that while dietary proteins are essential for good health, excessive protein intake can have negative effects on the body, such as increased stress on the kidneys and bones. Therefore, it's recommended to consume protein in moderation as part of a balanced and varied diet.

Protein deficiency, also known as protein-energy malnutrition (PEM), is a condition that occurs when an individual's diet fails to provide adequate amounts of protein and calories necessary for growth, maintenance, and repair of body tissues. Proteins are essential macromolecules that play critical roles in various bodily functions such as enzyme production, hormone regulation, immune response, and tissue structure.

There are two main types of protein deficiency disorders:

1. Marasmus: This is a chronic form of protein-energy malnutrition characterized by inadequate intake of both proteins and calories. It typically occurs in children from impoverished backgrounds who suffer from prolonged food deprivation. The body begins to break down its own tissues, including muscle mass, to meet energy demands, leading to severe weight loss, weakness, and delayed growth.

2. Kwashiorkor: This is an acute form of protein deficiency that primarily affects young children during weaning, when their diet transitions from breast milk to solid foods. While they may consume sufficient calories, these diets often lack adequate protein. Symptoms include edema (fluid accumulation in the abdomen and legs), distended bellies, skin lesions, hair changes, and impaired immune function.

In addition to these severe forms of protein deficiency, subclinical protein malnutrition can also occur when an individual's diet consistently provides insufficient protein levels over time. This can lead to reduced muscle mass, weakened immune function, and increased susceptibility to infections.

It is important to note that protein deficiency is relatively rare in developed countries where access to diverse food sources is generally available. However, specific populations such as elderly individuals, those with eating disorders, or those following restrictive diets may be at higher risk for developing protein deficiencies.

Protein hydrolysates are defined as proteins that have been broken down into smaller peptide chains or individual amino acids through a process called hydrolysis. This process involves the use of water, enzymes, or acids to break the bonds between the amino acids in the protein molecule.

Protein hydrolysates are often used in medical and nutritional applications because they are easier to digest and absorb than intact proteins. They are also less likely to cause allergic reactions or digestive discomfort in individuals who have difficulty tolerating whole proteins. Protein hydrolysates can be derived from a variety of sources, including animal proteins such as collagen and casein, as well as plant proteins such as soy and wheat.

In addition to their use in medical and nutritional applications, protein hydrolysates are also used in the food industry as flavor enhancers, emulsifiers, and texturizers. They are commonly found in products such as infant formula, sports drinks, and clinical nutrition formulas.

Soybean proteins are the proteins derived from soybeans, a legume native to East Asia. Soybeans contain approximately 40% protein by weight, making them a significant source of plant-based protein. The two major types of soy protein are:

1. Soy protein isolate (SPI): This is a highly refined protein that contains at least 90% protein by weight. It is made by removing carbohydrates and fiber from defatted soy flour, leaving behind a protein-rich powder. SPI is often used as an ingredient in various food products, including meat alternatives, energy bars, and beverages.
2. Soy protein concentrate (SPC): This type of soy protein contains approximately 70% protein by weight. It is made by removing some of the carbohydrates from defatted soy flour, leaving behind a higher concentration of proteins. SPC has applications in food and industrial uses, such as in textured vegetable protein (TVP) for meat alternatives, baked goods, and functional foods.

Soy proteins are considered high-quality proteins due to their complete amino acid profile, containing all nine essential amino acids necessary for human nutrition. They also have various health benefits, such as lowering cholesterol levels, improving bone health, and promoting muscle growth and maintenance. However, it is important to note that soy protein consumption should be balanced with other protein sources to ensure a diverse intake of nutrients.

Nutritive value is a term used to describe the amount and kind of nutrients, such as carbohydrates, proteins, fats, vitamins, minerals, and water, that a food provides. It refers to the ability of a food to supply the necessary components for growth, repair, maintenance, and energy in the body. The nutritive value of a food is usually expressed in terms of its content of these various nutrients per 100 grams or per serving. Foods with high nutritive value are those that provide a significant amount of essential nutrients in relation to their calorie content.

Vegetable proteins, also known as plant-based proteins, are nitrogenous organic compounds derived from plants. These proteins are composed of amino acid chains that are essential for the growth, repair, and maintenance of body tissues. Vegetable proteins can be found in a wide variety of plant sources such as legumes (e.g., beans, lentils, peas), grains (e.g., rice, wheat, corn), nuts, seeds, and vegetables.

It is important to note that while vegetable proteins are often considered "incomplete" because they may lack one or more of the essential amino acids found in animal-based proteins, consuming a variety of plant-based protein sources throughout the day can provide all the necessary amino acids for a healthy diet. Vegetarian and vegan diets that are well-planned can meet protein needs without the use of animal products.

Caseins are a group of phosphoproteins found in the milk of mammals, including cows and humans. They are the major proteins in milk, making up about 80% of the total protein content. Caseins are characterized by their ability to form micelles, or tiny particles, in milk when it is mixed with calcium. This property allows caseins to help transport calcium and other minerals throughout the body.

Caseins are also known for their nutritional value, as they provide essential amino acids and are easily digestible. They are often used as ingredients in infant formula and other food products. Additionally, caseins have been studied for their potential health benefits, such as reducing the risk of cardiovascular disease and improving bone health. However, more research is needed to confirm these potential benefits.

Nitrogen is not typically referred to as a medical term, but it is an element that is crucial to medicine and human life.

In a medical context, nitrogen is often mentioned in relation to gas analysis, respiratory therapy, or medical gases. Nitrogen (N) is a colorless, odorless, and nonreactive gas that makes up about 78% of the Earth's atmosphere. It is an essential element for various biological processes, such as the growth and maintenance of organisms, because it is a key component of amino acids, nucleic acids, and other organic compounds.

In some medical applications, nitrogen is used to displace oxygen in a mixture to create a controlled environment with reduced oxygen levels (hypoxic conditions) for therapeutic purposes, such as in certain types of hyperbaric chambers. Additionally, nitrogen gas is sometimes used in cryotherapy, where extremely low temperatures are applied to tissues to reduce pain, swelling, and inflammation.

However, it's important to note that breathing pure nitrogen can be dangerous, as it can lead to unconsciousness and even death due to lack of oxygen (asphyxiation) within minutes.

Digestion is the complex process of breaking down food into smaller molecules that can be absorbed and utilized by the body for energy, growth, and cell repair. This process involves both mechanical and chemical actions that occur in the digestive system, which includes the mouth, esophagus, stomach, small intestine, large intestine, and accessory organs such as the pancreas, liver, and gallbladder.

The different stages of digestion are:

1. Ingestion: This is the first step in digestion, where food is taken into the mouth.
2. Mechanical digestion: This involves physically breaking down food into smaller pieces through chewing, churning, and mixing with digestive enzymes.
3. Chemical digestion: This involves breaking down food molecules into simpler forms using various enzymes and chemicals produced by the digestive system.
4. Absorption: Once the food is broken down into simple molecules, they are absorbed through the walls of the small intestine into the bloodstream and transported to different parts of the body.
5. Elimination: The undigested material that remains after absorption is moved through the large intestine and eliminated from the body as feces.

The process of digestion is essential for maintaining good health, as it provides the necessary nutrients and energy required for various bodily functions.

Amino acids are organic compounds that serve as the building blocks of proteins. They consist of a central carbon atom, also known as the alpha carbon, which is bonded to an amino group (-NH2), a carboxyl group (-COOH), a hydrogen atom (H), and a variable side chain (R group). The R group can be composed of various combinations of atoms such as hydrogen, oxygen, sulfur, nitrogen, and carbon, which determine the unique properties of each amino acid.

There are 20 standard amino acids that are encoded by the genetic code and incorporated into proteins during translation. These include:

1. Alanine (Ala)
2. Arginine (Arg)
3. Asparagine (Asn)
4. Aspartic acid (Asp)
5. Cysteine (Cys)
6. Glutamine (Gln)
7. Glutamic acid (Glu)
8. Glycine (Gly)
9. Histidine (His)
10. Isoleucine (Ile)
11. Leucine (Leu)
12. Lysine (Lys)
13. Methionine (Met)
14. Phenylalanine (Phe)
15. Proline (Pro)
16. Serine (Ser)
17. Threonine (Thr)
18. Tryptophan (Trp)
19. Tyrosine (Tyr)
20. Valine (Val)

Additionally, there are several non-standard or modified amino acids that can be incorporated into proteins through post-translational modifications, such as hydroxylation, methylation, and phosphorylation. These modifications expand the functional diversity of proteins and play crucial roles in various cellular processes.

Amino acids are essential for numerous biological functions, including protein synthesis, enzyme catalysis, neurotransmitter production, energy metabolism, and immune response regulation. Some amino acids can be synthesized by the human body (non-essential), while others must be obtained through dietary sources (essential).

I'm sorry for any confusion, but "soybeans" are not a medical term. They are a type of legume that is commonly used in agriculture and food production. The medical community might discuss soybeans in the context of nutrition or allergies, but there isn't a formal medical definition for this term.

Here's some general information: Soybeans, scientifically known as Glycine max, are native to East Asia and are now grown worldwide. They are a significant source of plant-based protein and oil. Soybeans contain various nutrients, including essential amino acids, fiber, B vitamins, and minerals like calcium, iron, magnesium, and zinc. They are used in various food products such as tofu, soy milk, tempeh, and miso. Additionally, soybeans are also used in the production of industrial products, including biodiesel, plastics, and inks. Some people may have allergic reactions to soybeans or soy products.

"Macaca fascicularis" is the scientific name for the crab-eating macaque, also known as the long-tailed macaque. It's a species of monkey that is native to Southeast Asia. They are called "crab-eating" macaques because they are known to eat crabs and other crustaceans. These monkeys are omnivorous and their diet also includes fruits, seeds, insects, and occasionally smaller vertebrates.

Crab-eating macaques are highly adaptable and can be found in a wide range of habitats, including forests, grasslands, and wetlands. They are also known to live in close proximity to human settlements and are often considered pests due to their tendency to raid crops and steal food from humans.

These monkeys are social animals and live in large groups called troops. They have a complex social structure with a clear hierarchy and dominant males. Crab-eating macaques are also known for their intelligence and problem-solving abilities.

In medical research, crab-eating macaques are often used as animal models due to their close genetic relationship to humans. They are used in studies related to infectious diseases, neuroscience, and reproductive biology, among others.

Body weight is the measure of the force exerted on a scale or balance by an object's mass, most commonly expressed in units such as pounds (lb) or kilograms (kg). In the context of medical definitions, body weight typically refers to an individual's total weight, which includes their skeletal muscle, fat, organs, and bodily fluids.

Healthcare professionals often use body weight as a basic indicator of overall health status, as it can provide insights into various aspects of a person's health, such as nutritional status, metabolic function, and risk factors for certain diseases. For example, being significantly underweight or overweight can increase the risk of developing conditions like malnutrition, diabetes, heart disease, and certain types of cancer.

It is important to note that body weight alone may not provide a complete picture of an individual's health, as it does not account for factors such as muscle mass, bone density, or body composition. Therefore, healthcare professionals often use additional measures, such as body mass index (BMI), waist circumference, and blood tests, to assess overall health status more comprehensively.

"Inbred strains of rats" are genetically identical rodents that have been produced through many generations of brother-sister mating. This results in a high degree of homozygosity, where the genes at any particular locus in the genome are identical in all members of the strain.

Inbred strains of rats are widely used in biomedical research because they provide a consistent and reproducible genetic background for studying various biological phenomena, including the effects of drugs, environmental factors, and genetic mutations on health and disease. Additionally, inbred strains can be used to create genetically modified models of human diseases by introducing specific mutations into their genomes.

Some commonly used inbred strains of rats include the Wistar Kyoto (WKY), Sprague-Dawley (SD), and Fischer 344 (F344) rat strains. Each strain has its own unique genetic characteristics, making them suitable for different types of research.

An encyclopedia is a comprehensive reference work containing articles on various topics, usually arranged in alphabetical order. In the context of medicine, a medical encyclopedia is a collection of articles that provide information about a wide range of medical topics, including diseases and conditions, treatments, tests, procedures, and anatomy and physiology. Medical encyclopedias may be published in print or electronic formats and are often used as a starting point for researching medical topics. They can provide reliable and accurate information on medical subjects, making them useful resources for healthcare professionals, students, and patients alike. Some well-known examples of medical encyclopedias include the Merck Manual and the Stedman's Medical Dictionary.

Milk proteins are a complex mixture of proteins that are naturally present in milk, consisting of casein and whey proteins. Casein makes up about 80% of the total milk protein and is divided into several types including alpha-, beta-, gamma- and kappa-casein. Whey proteins account for the remaining 20% and include beta-lactoglobulin, alpha-lactalbumin, bovine serum albumin, and immunoglobulins. These proteins are important sources of essential amino acids and play a crucial role in the nutrition of infants and young children. Additionally, milk proteins have various functional properties that are widely used in the food industry for their gelling, emulsifying, and foaming abilities.

Immunoglobulin G (IgG) is a type of antibody, which is a protective protein produced by the immune system in response to foreign substances like bacteria or viruses. IgG is the most abundant type of antibody in human blood, making up about 75-80% of all antibodies. It is found in all body fluids and plays a crucial role in fighting infections caused by bacteria, viruses, and toxins.

IgG has several important functions:

1. Neutralization: IgG can bind to the surface of bacteria or viruses, preventing them from attaching to and infecting human cells.
2. Opsonization: IgG coats the surface of pathogens, making them more recognizable and easier for immune cells like neutrophils and macrophages to phagocytose (engulf and destroy) them.
3. Complement activation: IgG can activate the complement system, a group of proteins that work together to help eliminate pathogens from the body. Activation of the complement system leads to the formation of the membrane attack complex, which creates holes in the cell membranes of bacteria, leading to their lysis (destruction).
4. Antibody-dependent cellular cytotoxicity (ADCC): IgG can bind to immune cells like natural killer (NK) cells and trigger them to release substances that cause target cells (such as virus-infected or cancerous cells) to undergo apoptosis (programmed cell death).
5. Immune complex formation: IgG can form immune complexes with antigens, which can then be removed from the body through various mechanisms, such as phagocytosis by immune cells or excretion in urine.

IgG is a critical component of adaptive immunity and provides long-lasting protection against reinfection with many pathogens. It has four subclasses (IgG1, IgG2, IgG3, and IgG4) that differ in their structure, function, and distribution in the body.

... is found in the milk of many mammals. There are alpha and beta lactalbumins; both are contained in milk. Targeted ... Alpha-lactalbumin Beta-lactoglobulin Lactalbumin at the U.S. National Library of Medicine Medical Subject Headings (MeSH) ( ... Lactalbumin, also known as "whey protein", is the albumin contained in milk and obtained from whey. ... small scientific studies suggest that certain types of lactalbumin (whey protein) may improve immune responsiveness and ...
... , also known as LALBA, is a protein that in humans is encoded by the LALBA gene. α-Lactalbumin is a protein that ... As a result, pure α-lactalbumin will not form gels upon denaturation and acidification. α-Lactalbumin is a Ca2+ binding protein ... March 1995). "Lactation is disrupted by alpha-lactalbumin deficiency and can be restored by human alpha-lactalbumin gene ... These residue binding sites are conserved among most species containing α-lactalbumin. The sequence comparison of α-lactalbumin ...
... lactalbumin". Biochemistry. 28 (1): 7-13. doi:10.1021/bi00427a002. ISSN 0006-2960. PMID 2706269. Wu, Kuen-Phon; Weinstock, ...
"Alpha Lactalbumin - an overview , ScienceDirect Topics". www.sciencedirect.com. Retrieved 2022-04-28. "Alpha Lactalbumin - an ... In an acidic environment such as the stomach, alpha-lactalbumin unfolds into a different form and binds oleic acid to form a ... The principal proteins are alpha-lactalbumin, lactoferrin (apo-lactoferrin), IgA, lysozyme, and serum albumin. ...
as well as alpha-lactalbumin. 5) Alpha-lactalbumin was partially unfolded to allow for release of the calcium ion and ... 6) A patent for making HAMLET through combining alpha-lactalbumin with oleic acid was granted in 2008 (expired 2018). A patent ... Svensson M, Håkansson A, Mossberg AK, Linse S, Svanborg C (April 2000). "Conversion of alpha-lactalbumin to a protein inducing ... 3) Further experiments were made that isolated the compound multimeric alpha-lactalbumin (MAL) that caused the interesting ...
Plasma α-lactalbumin levels peak; and Decreased breast milk sodium concentration. Note that delayed onset of lactogenesis II is ...
Fitzgerald DK, Brodbeck U, Kiyosawa I, Mawal R, Colvin B, Ebner KE (Apr 1970). "Alpha-lactalbumin and the lactose synthetase ...
Alpha-lactalbumin, is a milk protein that acts as the regulatory subunit of lactose synthetase, acting to promote the ... Lysozyme type C and alpha-lactalbumin are similar both in terms of primary sequence and structure, and probably evolved from a ... Shewale JG, Sinha SK, Brew K (April 1984). "Evolution of alpha-lactalbumins. The complete amino acid sequence of the alpha- ... Stuart DI, Acharya KR, Walker NP, Smith SG, Lewis M, Phillips DC (1986). "Alpha-lactalbumin possesses a novel calcium binding ...
C-type lysozymes are closely related to α-lactalbumin in sequence and structure, making them part of the same glycoside ... McKenzie HA, White FH (1991). "Lysozyme and α-lactalbumin: structure, function, and interrelationships". Advances in Protein ...
One of the two molecules of this complex is multimeric alpha lactalbumin (MAL) (Figure 3), which was first discovered during a ... Svensson, M.; Håkansson, A.; Mossberg, A.-K.; Linse, S.; Svanborg, C. (2000-04-11). "Conversion of α-lactalbumin to a protein ... Human α-Lactalbumin Made Lethal to Tumor Cells)", Bioactive Components of Milk, Advances in Experimental Medicine and Biology, ...
HAMLET (Human Alpha-lactalbumin Made LEthal to Tumor cells) is a complex between alpha-lactalbumin and oleic acid that has been ... Endogenous human alpha-lactalbumin is complexed with a calcium ion and serves as a cofactor in lactose synthesis, but has no ... The alpha-lactalbumin must be partially unfolded to allow for release of the calcium ion and replacement with an oleic acid ... Alpha-lactalbumin is the primary protein component of human milk. In a 1995 study, it was discovered by Swedish scientist ...
It consists of N-acetyllactosamine synthase and alpha-lactalbumin. Alpha-lactalbumin, which is expressed in response to ... Alpha-lactalbumin is a Ca2+ binding protein specific to mammary glands. Beta-1,4-galactosyltransferase consists of the ... Alpha-lactalbumin promotes glucose binding to beta-1,4-galactosyltransferase. The beta-1,4-galactosyltransferase catalytic ... and protein-protein interactions for alpha-lactalbumin. Ramakrishnan B, Qasba PK (June 2001). "Crystal structure of lactose ...
It is a 5% solution of lactose in water, with some minerals and lactalbumin. The fat is removed and then processed for human ... Whey proteins consist primarily of α-lactalbumin and β-lactoglobulin. Sweet whey contains glycomacropeptide (GMP). It is also ... Whey proteins consist of α-lactalbumin, β-lactoglobulin, serum albumin, immunoglobulins, and proteose peptones. Whey protein is ... This protein is typically a mixture of beta-lactoglobulin (~48-58%), alpha-lactalbumin (~13-19%), bovine serum albumin (~6%)( ...
They have been isolated from human hair, lactalbumin, and feathers. Lanthionines have also been found in bacterial cell walls ...
Lactalbumin, or whey protein, is a protein fraction of milk. It is mainly Beta-lactoglobulin, although serum albumin also ... See § Other albumin types for lactalbumin, ovalbumin and plant "2S albumin". Albumins in general are transport proteins that ...
Human alpha-lactalbumin is a natural protein component of HBM. It can be extracted by chromatography from breast milk. It ... complexes with oleic acid to form a protein called the "human alpha-lactalbumin made lethal to tumor cells" (HAMLET). The ...
Arai M, Kuwajima K (1996). "Rapid formation of a molten globule intermediate in refolding of alpha-lactalbumin". Folding & ... alpha-lactalbumin, barstar, and staphylococcal nuclease. However, because experimental evidence of early folding events is ...
The proteins consist of α-lactalbumin, β-lactoglobulin, serum albumin and immunoglobulins. Glycomacropeptide also makes up the ... This protein is typically a mixture of beta-lactoglobulin (~65%), alpha-lactalbumin (~25%), bovine serum albumin (~8%) (see ... "Food compositions comprising one or both of recombinant beta-lactoglobulin protein and recombinant alpha-lactalbumin protein", ...
"Dynamic regimes and correlated structural dynamics in native and denatured alpha-lactalbumin". Journal of Molecular Biology. ...
Dairy-sourced protein ingredients include casein, caseinates, whey and lactalbumin, among others. The U.S. FDA has a recall ... and κ-casein from casein proteins and α-lactalbumin and β-lactoglobulin from whey proteins. There is some cross-reactivity with ...
Sato T, Aoki N, Matsuda T, Furukawa K (1998). "Differential effect of alpha-lactalbumin on beta-1,4-galactosyltransferase IV ...
Shea, A. P.; Crofcheck, C. L.; Payne, F. A.; Xiong, Y. L. (2009). "Foam fractionation of α-lactalbumin and β-lactoglobulin from ... The table compares foam separation to other techniques used to separate the protein, α-lactalbumin, from a whey protein ... "Ultrafiltration Modes of Operation for the Separation of A-lactalbumin from Acid Casein Whey." Journal of Membrane Science 153 ... "Whey Protein Isolate and -Lactalbumin Recovery from Lactic Acid Whey Using Cation-Exchange Chromatography." Journal of Food ...
"Dynamic regimes and correlated structural dynamics in native and denatured alpha-lactalbumin". Journal of Molecular Biology. ...
2018). "alpha-Lactalbumin effect on myo-inositol intestinal absorption: in vivo and in vitro". Current Drug Delivery. 15 (9): ... A recent study reported that the myo-inositol and α-lactalbumin combination is able to increase myo-inositol plasmatic content ... A possible solution could be represented by the combination of myo-inositol and α-lactalbumin. This combination shows a ... 2018). "Effects of myo-inositol plus alpha-lactalbumin in myo-inositol-resistant PCOS women". Journal of Ovarian Research. 11 ( ...
... with molten globule states of bovine alpha-lactalbumin". J. Biol. Chem. 272 (44): 27722-9. doi:10.1074/jbc.272.44.27722. PMID ...
This makes them the third largest fraction of whey protein isolate, after alpha-lactalbumin and beta-lactoglobulin. GMP is ...
Its substrate specificity is affected by alpha-lactalbumin but it is not expressed in lactating mammary tissue. Two transcript ...
HAMLET (human alpha-lactalbumin made lethal to tumor cells) is a molecular complex derived from human breast milk that kills ... Human α-Lactalbumin Made Lethal to Tumor Cells)". Bioactive Components of Milk. Advances in Experimental Medicine and Biology. ...
Its expression is altered by various cancer-treatment compounds: human alpha-lactalbumin made lethal to tumor cells; oleate ...
The Tīrau dairy factory is New Zealand's only producer of lactalbumin, a key ingredient in the production of sports supplements ...
Lactalbumin is found in the milk of many mammals. There are alpha and beta lactalbumins; both are contained in milk. Targeted ... Alpha-lactalbumin Beta-lactoglobulin Lactalbumin at the U.S. National Library of Medicine Medical Subject Headings (MeSH) ( ... Lactalbumin, also known as "whey protein", is the albumin contained in milk and obtained from whey. ... small scientific studies suggest that certain types of lactalbumin (whey protein) may improve immune responsiveness and ...
Physicochemical Characterisation of β-Carotene Emulsion Stabilised by Covalent Complexes of α-Lactalbumin with (−)- ...
Alpha Lactalbumin Market: Report Scope A latest market report by Persistence Market Research on the global alpha lactalbumin ... Alpha-Lactalbumin to Witness a Potential Growth in the Sports Nutrition Industry. ... Alpha Lactalbumin Market: Report Scope. A latest market report by Persistence Market Research on the global alpha lactalbumin ... Alpha Lactalbumin Market: Report Scope. A latest market report by Persistence Market Research on the global alpha lactalbumin ...
amino acid nitrogen absorption, intestinal perfusion, lactalbumin hydrolysate, peptide absorption, peptide chain length ... Effect of peptide chain length on amino acid and nitrogen absorption from two lactalbumin hydrolysates in the normal human ... 2. Copper-chelation chromatography showed that one lactalbumin hydrolysate (LH2) contained 98% peptides with a chain length , 4 ... Effect of peptide chain length on amino acid and nitrogen absorption from two lactalbumin hydrolysates in the normal human ...
Isolation and characterization of the mouse alpha-lactalbumin-encoding gene: interspecies comparison, tissue- and stage- ... Expression of a bovine alpha-lactalbumin transgene in alpha-lactalbumin-deficient mice can rescue lactation. In vivo ... Bleck, G.T.; Bremel, R.D. 1990: Isolation and cloning of a gene encoding bovine alpha -lactalbumin Journal of Dairy Science 73( ... Vilotte, J.L.; Soulier, S.; Mercier, J.C. 1992: Sequence of the murine α-lactalbumin-encoding cDNA : interspecies comparison of ...
"Lactalbumin" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical Subject ... This graph shows the total number of publications written about "Lactalbumin" by people in UAMS Profiles by year, and whether " ... Below are the most recent publications written about "Lactalbumin" by people in Profiles over the past ten years. ...
Got Stress? Alpha-Lactalbumin to the Rescue. Most people these days will tell you that they are stressed! Chronic stress has ...
Milk proteins with a nutritional role in the infant: α-lactalbumin and bioactive peptides.. Activity: Talk or presentation ...
Labshub completely concentrates on constant progress and monitoring ensures that we can deliver all assistance at a consistently high-quality level, via our disciplined and automated processes, which is why we are here 24/7 and 365 days for your services. ...
However, the high resolution x-ray crystal structure of human alpha-lactalbumin-Zn2+ complex at 1.7-A resolution (pH 7.6) does ... The Zn2+ ion binds specifically in the cleft of alpha-lactalbumin (the region which forms the active site of the homologous ... It has been proposed that the binding of Zn2+ to alpha-lactalbumin switches the conformation to one akin to a state ... It has been proposed that the binding of Zn2+ to alpha-lactalbumin switches the conformation to one akin to a state ...
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Home / Test menu / Individual tests / Specific IgG4 / Milk Cow nBos D 4 (Native, Alpha-Lactalbumin) (F76). ... Specific IgG4 / Milk Cow nBos D 4 (Native, Alpha-Lactalbumin) (F76). F76S ...
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4-GALACTOSYLTRANSFERASE COMPLEX WITH ALPHA-LACTALBUMIN AND N-BUTANOYL-GLUCOAMINE ... BETA-1,4-GALACTOSYLTRANSFERASE COMPLEX WITH ALPHA-LACTALBUMIN AND N-BUTANOYL-GLUCOAMINE Coordinates. PDB Format Method. X-RAY ... Ramakrishnan, B. et al., ALPHA-LACTALBUMIN (LA) STIMULATES MILK BETA-1,4-GALACTOSYLTRANSFERASE I (BETA 4GAL-T1) TO TRANSFER ...
4-galactosyltransferase-I in complex with alpha-lactalbumin, Ca and UDP-galactose ... Crystal structure of the catalytic domain of bovine beta1,4-galactosyltransferase-I in complex with alpha-lactalbumin, Ca and ...
Lactalbumin is produced by precipitating whey proteins. Heat and changes in pH may be used to denature the whey proteins so ...
Return to Article Details FAST PROTEIN LIQUID CHROMATOGRAPHY OF CAMEL α-LACTALBUMIN FRACTION WITH RADICAL SCAVENGING ACTIVITY ...
The refolding of bovine alpha-lactalbumin (BLA) from its chemically denatured state in 6 M GuHCl has been investigated by a ... The refolding of bovine alpha-lactalbumin (BLA) from its chemically denatured state in 6 M GuHCl has been investigated by a ... Rapid collapse and slow structural reorganisation during the refolding of bovine alpha-lactalbumin. ... Rapid collapse and slow structural reorganisation during the refolding of bovine alpha-lactalbumin. ...
Alpha-Lactalbumin II-34. Application Areas of Whey and Whey Proteins II-34. Body Composition and Weight Management II-34. ...
Complexes of α-lactalbumin and five different fatty acids (vaccenic, linoleic, palmitoleic, stearic, and elaidic acid) were ... The cytotoxicity of all the variants is similar to that previously determined for α-lactalbumin/oleic acid complexes.. en_GB. ... The amount of fatty acid per α-lactalbumin molecule was found to correlate with the cytotoxicity; the higher the number of ... Complexes of the milk protein, α-lactalbumin, and the fatty acid, oleic acid, have previously been shown to be cytotoxic. ...
lactalbumin / whey / purity / ultrafiltration Mots clés : -lactalbumine / lactosérum / pureté / ultrafiltration Correspondence ... lactalbumin with ultrafiltration ceramic membranes from acid casein whey: study of operating conditions Arabelle Mullera, ... lactalbumin ( -LA) is to perform a two-step cascade. The first step of pre-purifying presented herein, consists of ... Purification of $\alpha$-lactalbumin from a prepurified acid whey: Ultrafiltration or precipitation Lait 83, 439-451 (2003). ...
lactalbumin, lactalbumin phosphate, lactoglobulin, lactoferrin. *recaldent (found in some toothpastes). *rennet. *tagatose (a ...
Atomically detailed description of the unfolding of α-lactalbumin by the combined use of experiments and simulations. Journal ... Atomically detailed description of the unfolding of α-lactalbumin by the combined use of experiments and simulations. In: ... Dive into the research topics of Atomically detailed description of the unfolding of α-lactalbumin by the combined use of ... Atomically detailed description of the unfolding of α-lactalbumin by the combined use of experiments and simulations. / ...
Preparation of enzymatically cross-linked α-lactalbumin nanoparticles and their appli Preparation of enzymatically cross- ... Our hypothesis is that enzymatically crosslinked α-lactalbumin (ALA) nanoparticles (ALATGs) prepared using transglutaminase ... linked α-lactalbumin nanoparticles and their application for encapsulating lycopene. Guo, Siqi; Guo, Qing; Zhang, Yifan; Peng, ...
lactalbumin / whey protein / -amino acid / calcium phosphorus / digestion Mots clés : -lactalbumine / protéines de lactosérum ... lactalbumin and whey protein concentrate on -amino acids, calcium and phosphorus levels in blood and gastrointestinal tract of ... lactalbumin (. -la) or whey protein concentrate (WPC) for two weeks. The results indicated that the concentrations of calcium ...
Efficacy of α-lactalbumin and milk protein on weight loss and body composition during energy restriction. Obesity. 2011 Feb 1; ... Efficacy of α-lactalbumin and milk protein on weight loss and body composition during energy restriction. / Soenen, Stijn; ... Efficacy of α-lactalbumin and milk protein on weight loss and body composition during energy restriction. ... Dive into the research topics of Efficacy of α-lactalbumin and milk protein on weight loss and body composition during energy ...
Lactalbumin Hydrolysate Solution (50X). Lactalbumin Hydrolysate Solution (50X), concentration: 166.6 g/l. 10 x 100 mL Learn ...
The ASCIA diet sheet - general information should be printed in conjunction with the ASCIA diet sheet for cows milk protein (dairy) allergy.
  • Milk proteins with a nutritional role in the infant: α-lactalbumin and bioactive peptides. (ku.dk)
  • Lactalbumin is produced by precipitating whey proteins. (adpi.org)
  • A theoretical approach to possible biological functions of the milk-whey proteins, alpha-lactalbumin and beta-lactoglobulin. (ncsu.edu)
  • Considered a byproduct, the globe-like proteins contained in whey include lactalbumin, lactoferrin and immunoglobulins . (livestrong.com)
  • HAMLET (Human Alpha-lactalbumin Made Lethal to Tumour cells) is a compound of proteins and lipids (fats and fat-like substances) from breast milk. (lu.se)
  • The Zn2+ ion binds specifically in the "cleft" of alpha-lactalbumin (the region which forms the active site of the homologous protein lysozyme). (ox.ac.uk)
  • Fig. 1 Crystal structures of human -lactal- bumin (PDB file 1HML), lysozyme (2LZT) and ribonuclease A (7RSA) showing potentially long-lived internal water molecules, disul- fide bonds (yellow), and the Ca2+ ion (green) in -lactalbumin. (lu.se)
  • Complexes of the milk protein, α-lactalbumin, and the fatty acid, oleic acid, have previously been shown to be cytotoxic. (teagasc.ie)
  • Complexes of α-lactalbumin and five different fatty acids (vaccenic, linoleic, palmitoleic, stearic, and elaidic acid) were prepared and compared to those formed with oleic acid. (teagasc.ie)
  • The cytotoxic effect of complexes between α-lactalbumin and linoleic acid, vaccenic acid, or oleic acid was further investigated using flow cytometry and found to induce cell death resembling apoptosis on Jurkat cells. (teagasc.ie)
  • The cytotoxicity of all the variants is similar to that previously determined for α-lactalbumin/oleic acid complexes. (teagasc.ie)
  • LEthal to Tumour cells protein, or HAMLET for short, is a protein complex found at high levels in human breast milk made up of the protein alpha-lactalbumin and a fatty acid, oleic acid. (thenakedscientists.com)
  • Lactalbumin, also known as "whey protein", is the albumin contained in milk and obtained from whey. (wikipedia.org)
  • Targeted small scientific studies suggest that certain types of lactalbumin (whey protein) may improve immune responsiveness and increase levels of glutathione systemically in animals and which apparently possess antiviral (against viruses), anti-apoptotic (impede cell death) and anti-tumor (against cancers or tumors) activities in humans, but larger and better studies are needed to confirm these attributions. (wikipedia.org)
  • Alpha-lactalbumin possesses a distinct zinc binding site. (ox.ac.uk)
  • Practical applications: Cytotoxic complexes of α-lactalbumin and several different fatty acids could be produced. (teagasc.ie)
  • 1. A double lumen jejunal perfusion technique has been used in man to study the effect of peptide chain length on absorption of amino acid nitrogen from two partial enzymic hydrolysates of lactalbumin. (portlandpress.com)
  • Our objective was to examine whether elevated α-lactalbumin (αlac) protein intake compared to elevated supra sustained milk protein (SSP) and sustained milk protein (SP) intake results into a difference in body weight and body composition over a 6-month energy-restriction intervention. (edu.au)
  • aminés, en calcium et en phosphore dans le plasma et le tube digestif chez les rats. (edpsciences.org)
  • The murine alpha-lactalbumin-encoding gene (m alpha La) was isolated and completely sequenced. (eurekamag.com)
  • It has been proposed that the binding of Zn2+ to alpha-lactalbumin switches the conformation to one akin to a state intermediate in the folding of the protein. (ox.ac.uk)
  • However, the high resolution x-ray crystal structure of human alpha-lactalbumin-Zn2+ complex at 1.7-A resolution (pH 7.6) does not reveal any significant change in conformation from the native state. (ox.ac.uk)
  • Rapid collapse and slow structural reorganisation during the refolding of bovine alpha-lactalbumin. (ox.ac.uk)
  • The refolding of bovine alpha-lactalbumin (BLA) from its chemically denatured state in 6 M GuHCl has been investigated by a variety of complementary biophysical approaches. (ox.ac.uk)
  • We can make the same complex with cows' milk alpha-lactalbumin. (thenakedscientists.com)
  • Multimeric alpha-lactalbumin. (lu.se)
  • Multimeric alpha-lactalbumin killed all transformed, embryonic, and lymphoid cells tested but spared mature epithelial elements. (lu.se)
  • Finally, analysis of the mechanism by which multimeric alpha-lactalbumin induces apoptosis in transformed epithelial cells could lead to the design of antitumor agents. (lu.se)
  • That protein is called Alpha-lactalbumin. (clevelandclinic.org)
  • The effects of alpha-lactalbumin and glycomacropeptide on the association of CaCo-2 cells by enteropathogenic Escherichia coli, Salmonella typhimurium and Shigella flexneri. (webmd.com)
  • Lactalbumin is found in the milk of many mammals. (wikipedia.org)
  • This graph shows the total number of publications written about "Lactalbumin" by people in UAMS Profiles by year, and whether "Lactalbumin" was a major or minor topic of these publications. (uams.edu)
  • Below are the most recent publications written about "Lactalbumin" by people in Profiles over the past ten years. (uams.edu)
  • 15. Alpha-lactalbumin unfolding is not sufficient to cause apoptosis, but is required for the conversion to HAMLET (human alpha-lactalbumin made lethal to tumor cells). (nih.gov)
  • Two proteins isolated from breast milk are showing promise as antibiotics: lactoferrin, which is also active against viruses and fungal infections as well as bacteria, and HAMLET - Human Alpha-lactalbumin Made Lethal to Tumor Cells, which is active against tumour cells. (dailymail.co.uk)
  • Quantitative PCR analysis revealed ∼50% reduction in the expression of key lactogenesis mammary genes including whey acid protein, α-lactalbumin, and β-casein. (nih.gov)
  • The ability of noncovalently immobilized nisin to withstand exchange by the milk proteins bovine serum albumin, β-lactoglobulin, α-lactalbumin, and β-casein on surfaces that had been silanized with dichlorodiethylsilane to exhibit high and low. (oregonstate.edu)
  • The IgA antibodies were measured in serum against gluten, gliadin, lactoglobulin, lactalbumin, casein and ovalbumin in patients with MS and controls using ELISA technique. (greenmedinfo.com)
  • Lactalbumin is found in the milk of many mammals. (wikipedia.org)
  • α-lactalbumin is a known immunomodulator present in human milk. (wyethnutritionsc.org)
  • In milk and egg, being allergic to only α-lactalbumin, β-lactoglobulin, or ovalbumin may indicate that you'll be able to tolerate baked forms of milk and eggs but not raw forms. (thermofisher.com)
  • 18. Divergent Anticancer Activity of Free and Formulated Camel Milk α-Lactalbumin. (nih.gov)
  • To achieve these aims, we first fitted a mixed Bayesian multitrait genomic model to infer the genomic correlations among 6 milk nitrogen fractions [4 caseins (CN), namely κ-, β-, α S1 -, and α S2 -CN, and 2 whey proteins, namely β-lactoglobulin (β-LG) and α-lactalbumin (α-LA)], in a population of 989 Italian Brown Swiss cows. (nih.gov)
  • This gene encodes alpha-lactalbumin, a principal protein of milk. (nih.gov)
  • 11. Molten globule of bovine alpha-lactalbumin at neutral pH induced by heat, trifluoroethanol, and oleic acid: a comparative analysis by circular dichroism spectroscopy and limited proteolysis. (nih.gov)
  • 17. Comparative study on heat stability of camel and bovine apo and holo alpha-lactalbumin. (nih.gov)
  • 19. [Structure and Anti-Tumor Activity of Bovine α-Lactalbumin after Binding Linoleic Acid]. (nih.gov)
  • The dendrimer was found to be superior to the imidazoquinoline monomer in inducing high titers of high-affinity antibodies to bovine α-lactalbumin. (ku.edu)
  • Native α-lactalbumin (Protein Data Bank ID: 1B9O) undergoes a depletion of calcium and binds to oleic acids to form HAMLET. (medscape.com)
  • While partial unfolding of α-lactalbumin is an essential feature of HAMLET formation, the structure of the HAMLET complex is not fully understood. (medscape.com)
  • 12. No need to be HAMLET or BAMLET to interact with histones: binding of monomeric alpha-lactalbumin to histones and basic poly-amino acids. (nih.gov)
  • A folding variant of alpha-lactalbumin, called HAMLET, likely induces apoptosis in tumor and immature cells. (nih.gov)
  • Alpha-lactalbumin and beta-lactoglobulin form the major protein constituents of whey. (justia.com)
  • natural source of lactalbumin and immunoglobulinsnnProtein Powder is a highly efficient, advanced protein enhancement product. (fairwaymarket.com)
  • 7. Cytotoxic aggregates of alpha-lactalbumin induced by unsaturated fatty acid induce apoptosis in tumor cells. (nih.gov)
  • Because on an industrial scale a complete separation of alpha-lactalbumin and beta-lactoglobulin is difficult, the implication is that cost effective alpha-lactalbumin preparations will contain beta-lactoglobulin as well. (justia.com)
  • So obviously any contamination of the alpha-lactalbumin preparation with beta-lactoglobulin, will dramatically lower the Trp/LNAA ratio of the final product. (justia.com)
  • As mentioned, alpha-lactalbumin as well as its hydrolysates have gained popularity as a safe option to enhance plasma tryptophan levels. (justia.com)
  • Alpha-lactalbumin forms the regulatory subunit of the lactose synthase (LS) heterodimer and beta 1,4-galactosyltransferase (beta4Gal-T1) forms the catalytic component. (nih.gov)
  • 9. Heat-treatment method for producing fatty acid-bound alpha-lactalbumin that induces tumor cell death. (nih.gov)
  • Probing subtle differences in the hydrogen exchange behavior of variants of the human alpha-lactalbumin molten globule using mass spectrometry. (ox.ac.uk)
  • The hydrogen-exchange behavior of the low-pH molten globule of human alpha-lactalbumin, containing all four disulfides, has been examined and compared with that of a single disulfide variant, [28-111] alpha-lactalbumin, and of a series of proline variants of [28-111] alpha-lactalbumin. (ox.ac.uk)
  • As a monomer, alpha-lactalbumin strongly binds calcium and zinc ions and may possess bactericidal or antitumor activity. (nih.gov)
  • Alpha-lactalbumin and tryptophan have been tested for various measures of overnight recovery, sleep quality and quantity, morning wakefulness and cognitive performance. (milkspecialties.com)
  • Alpha-lactalbumin preparations are readily available and have a relatively high tryptophan concentration. (justia.com)
  • However, the use of alpha-lactalbumin as a starting point for tryptophan-rich preparations, comes with disadvantages in terms of maximal Trp/LNAA ratios and costs. (justia.com)
  • [ 33 ] The crystal structure of human α-lactalbumin [ 34 ] reveals a large α-helical domain with three major α-helices and two short 3 10 -helices. (medscape.com)
  • 14. Gastric digestion of α-lactalbumin in adult human subjects using capsule endoscopy and nasogastric tube sampling. (nih.gov)
  • [ 9 , 26 ] However, native α-lactalbumin was shown to lack tumoricidal activity and no post-translational modifications explaining the new activity were found. (medscape.com)
  • 1. Structure and stability analysis of cytotoxic complex of camel α-lactalbumin and unsaturated fatty acids produced at high temperature. (nih.gov)

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