The metal-free red phycobilin pigment in a conjugated chromoprotein of red algae. It functions as a light-absorbing substance together with chlorophylls.
Light energy harvesting structures attached to the THYLAKOID MEMBRANES of CYANOBACTERIA and RED ALGAE. These multiprotein complexes contain pigments (PHYCOBILIPROTEINS) that transfer light energy to chlorophyll a.
The metal-free blue phycobilin pigment in a conjugated chromoprotein of blue-green algae. It functions as light-absorbing substance together with chlorophylls.
Linear TETRAPYRROLES that give a characteristic color to BILE including: BILIRUBIN; BILIVERDIN; and bilicyanin.
Any normal or abnormal coloring matter in PLANTS; ANIMALS or micro-organisms.
Open chain tetrapyrroles that function as light harvesting chromophores in PHYCOBILIPROTEINS.
A phylum of oxygenic photosynthetic bacteria comprised of unicellular to multicellular bacteria possessing CHLOROPHYLL a and carrying out oxygenic PHOTOSYNTHESIS. Cyanobacteria are the only known organisms capable of fixing both CARBON DIOXIDE (in the presence of light) and NITROGEN. Cell morphology can include nitrogen-fixing heterocysts and/or resting cells called akinetes. Formerly called blue-green algae, cyanobacteria were traditionally treated as ALGAE.
Plants of the division Rhodophyta, commonly known as red algae, in which the red pigment (PHYCOERYTHRIN) predominates. However, if this pigment is destroyed, the algae can appear purple, brown, green, or yellow. Two important substances found in the cell walls of red algae are AGAR and CARRAGEENAN. Some rhodophyta are notable SEAWEED (macroalgae).
A genus of RED ALGAE in the family Bangiaceae. It is the most widely consumed SEAWEED in the world and especially in Asia.
Complexes containing CHLOROPHYLL and other photosensitive molecules. They serve to capture energy in the form of PHOTONS and are generally found as components of the PHOTOSYSTEM I PROTEIN COMPLEX or the PHOTOSYSTEM II PROTEIN COMPLEX.
Four PYRROLES joined by one-carbon units linking position 2 of one to position 5 of the next. The conjugated bond system results in PIGMENTATION.
One of the three domains of life (the others being BACTERIA and ARCHAEA), also called Eukarya. These are organisms whose cells are enclosed in membranes and possess a nucleus. They comprise almost all multicellular and many unicellular organisms, and are traditionally divided into groups (sometimes called kingdoms) including ANIMALS; PLANTS; FUNGI; and various algae and other taxa that were previously part of the old kingdom Protista.
A class of EUKARYOTA (traditionally algae), characterized by biflagellated cells and found in both freshwater and marine environments. Pigmentation varies but only one CHLOROPLAST is present. Unique structures include a nucleomorph and ejectosomes.
That portion of the electromagnetic spectrum in the visible, ultraviolet, and infrared range.
Light harvesting proteins found in phycobilisomes.
Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which VEGETABLE PROTEINS is available.

Quantifying aggregation of IgE-FcepsilonRI by multivalent antigen. (1/197)

Aggregation of cell surface receptors by multivalent ligand can trigger a variety of cellular responses. A well-studied receptor that responds to aggregation is the high affinity receptor for IgE (FcepsilonRI), which is responsible for initiating allergic reactions. To quantify antigen-induced aggregation of IgE-FcepsilonRI complexes, we have developed a method based on multiparameter flow cytometry to monitor both occupancy of surface IgE combining sites and association of antigen with the cell surface. The number of bound IgE combining sites in excess of the number of bound antigens, the number of bridges between receptors, provides a quantitative measure of IgE-FcepsilonRI aggregation. We demonstrate our method by using it to study the equilibrium binding of a haptenated fluorescent protein, 2,4-dinitrophenol-coupled B-phycoerythrin (DNP25-PE), to fluorescein isothiocyanate-labeled anti-DNP IgE on the surface of rat basophilic leukemia cells. The results, which we analyze with the aid of a mathematical model, indicate how IgE-FcepsilonRI aggregation depends on the total concentrations of DNP25-PE and surface IgE. As expected, we find that maximal aggregation occurs at an optimal antigen concentration. We also find that aggregation varies qualitatively with the total concentration of surface IgE as predicted by an earlier theoretical analysis.  (+info)

Differential kappa-opioid receptor expression on mouse lymphocytes at varying stages of maturation and on mouse macrophages after selective elicitation. (2/197)

The combination of indirect immunofluorescent labeling and flow cytometry has proven to be a sensitive method for labeling of the kappa-opioid receptor on mouse thymocytes. In the present study, this labeling procedure was applied, along with phenotypic analysis, to mature immune cell populations to determine whether kappa-opioid receptor expression is present after immune cell maturation. Unfixed primary splenocytes from 6- to 8-week-old C57BL/6ByJ male mice were incubated with the fluorescein-containing, kappa-selective ligand fluorescein-conjugated 2-(3, 4-dichlorophenyl)-N-methyl-N-[1-(3-aminophenyl)-2-(1-pyrrolidinyl)eth yl]acetamide (FITC-AA). Amplification of FITC-AA binding to the kappa-opioid receptor was attained by adding a biotin-conjugated antifluorescein antibody, followed by extravidin-R-phycoerythrin. It has been shown previously that greater than 60% of immature thymocytes (CD4(+)/CD8(+)) demonstrated specific kappa-opioid receptor labeling. However, the present report shows that less than 25% of either T-helper or T-cytotoxic splenic lymphocytes expressed the kappa-opioid receptor. Likewise, only 16% of all splenic B lymphocytes were labeled for the kappa-opioid receptor. These findings demonstrate a decrease in kappa-opioid receptor expression on maturation of mouse lymphocytes. Interestingly, resident peritoneal macrophages showed a greater magnitude of specific receptor labeling, compared with either thymocytes or splenocytes, and approximately 50% of the resting Mphi expressed the kappa-opioid receptor. However, elicitation of Mphi with thioglycollate resulted in the complete loss of the expression of this receptor. Taken together, these findings demonstrate the diversity in the expression of the kappa-opioid receptor on immune cells at varying stages of differentiation, with preferential expression demonstrated by resident, peritoneal macrophages.  (+info)

Diel rhythms in ribulose-1,5-bisphosphate carboxylase/oxygenase and glutamine synthetase gene expression in a natural population of marine picoplanktonic cyanobacteria (Synechococcus spp.). (3/197)

Diel periodicity in the expression of key genes involved in carbon and nitrogen assimilation in marine Synechococcus spp. was investigated in a natural population growing in the surface waters of a cyclonic eddy in the northeast Atlantic Ocean. Synechococcus sp. cell concentrations within the upper mixed layer showed a net increase of three- to fourfold during the course of the experiment (13 to 22 July 1991), the population undergoing approximately one synchronous division per day. Consistent with the observed temporal pattern of phycoerythrin (CpeBA) biosynthesis, comparatively little variation was found in cpeBA mRNA abundance during either of the diel cycles investigated. In marked contrast, the relative abundance of transcripts originating from the genes encoding the large subunit of ribulose bisphosphate carboxylase/oxygenase (rbcL) and glutamine synthetase (glnA) showed considerable systematic temporal variation and oscillated during the course of each diel cycle in a reciprocal rhythm. Whereas activation of rbcL transcription was clearly not light dependent, expression of glnA appeared sensitive to endogenous changes in the physiological demands for nitrogen that arise as a natural consequence of temporal periodicity in photosynthetic carbon assimilation. The data presented support the hypothesis that a degree of temporal separation may exist between the most active periods of carbon and nitrogen assimilation in natural populations of marine Synecoccoccus spp.  (+info)

Evolution of a light-harvesting protein by addition of new subunits and rearrangement of conserved elements: crystal structure of a cryptophyte phycoerythrin at 1.63-A resolution. (4/197)

Cryptophytes are unicellular photosynthetic algae that use a lumenally located light-harvesting system, which is distinct from the phycobilisome structure found in cyanobacteria and red algae. One of the key components of this system is water-soluble phycoerythrin (PE) 545 whose expression is enhanced by low light levels. The crystal structure of the heterodimeric alpha(1)alpha(2)betabeta PE 545 from the marine cryptophyte Rhodomonas CS24 has been determined at 1.63-A resolution. Although the beta-chain structure is similar to the alpha and beta chains of other known phycobiliproteins, the overall structure of PE 545 is novel with the alpha chains forming a simple extended fold with an antiparallel beta-ribbon followed by an alpha-helix. The two doubly linked beta50/beta61 chromophores (one on each beta subunit) are in van der Waals contact, suggesting that exciton-coupling mechanisms may alter their spectral properties. Each alpha subunit carries a covalently linked 15,16-dihydrobiliverdin chromophore that is likely to be the final energy acceptor. The architecture of the heterodimer suggests that PE 545 may dock to an acceptor protein via a deep cleft and that energy may be transferred via this intermediary protein to the reaction center.  (+info)

Fluorescence polarization studies on four biliproteins and a bilin model for phycoerythrin 545. (5/197)

Fluorescence (excitation) polarization spectroscopy in the wavelength region of the bilin chromophores was applied to phycoerythrocyanin (CV-phycocyanin), phycocyanins 645 and 612, and phycoerythrin 545. The cryptomonad biliproteins - phycoerythrin 545 and phycocyanins 612 and 645 - were studied as both protein dimers having an alpha(2)beta(2) polypeptide structure and as alphabeta monomers. The cyanobacterial phycoerythrocyanin (CV-phycocyanin) was a trimeric oligomer. The changes in polarization across the spectrum were attributed to transfers of energy between bilins. Cryptomonad biliproteins are isolated as dimers. The similarities between their steady-state fluorescence polarization spectra and those of the corresponding monomers suggested that the monomers' conformations were analogous to the dimers. This supports the use of monomers in the study of dimer bilin organization. The unusual polarization spectrum of phycoerythrin 545 was explained using a model for the topography of its bilins. Obtaining the emission spectra of phycoerythrin 545 at several temperatures and a deconvolution of the dimer circular dichroism spectrum also successfully tested the bilin model. Circular dichroism spectroscopy was used to determine which polarization changes are formed by Forster resonance energy transfers and which may be produced by internal conversions between high- and low-energy states of pairs of exciton-coupled bilins. Attempts were made to assign energy transfer events to the corresponding changes in fluorescence polarization for each of the four biliproteins.  (+info)

Molecular structure, localization and function of biliproteins in the chlorophyll a/d containing oxygenic photosynthetic prokaryote Acaryochloris marina. (6/197)

We investigated the localization, structure and function of the biliproteins of the oxygenic photosynthetic prokaryote Acaryochloris marina, the sole organism known to date that contains chlorophyll d as the predominant photosynthetic pigment. The biliproteins were isolated by means of sucrose gradient centrifugation, ion exchange and gel filtration chromatography. Up to six biliprotein subunits in a molecular mass range of 15.5-18.4 kDa were found that cross-reacted with antibodies raised against phycocyanin or allophycocyanin from a red alga. N-Terminal sequences of the alpha- and beta-subunits of phycocyanin showed high homogeneity to those of cyanobacteria and red algae, but not to those of cryptomonads. As shown by electron microscopy, the native biliprotein aggregates are organized as rod-shaped structures and located on the cytoplasmic side of the thylakoid membranes predominantly in unstacked thylakoid regions. Biochemical and spectroscopic analysis revealed that they consist of four hexameric units, some of which are composed of phycocyanin alone, others of phycocyanin together with allophycocyanin. Spectroscopic analysis of isolated photosynthetic reaction center complexes demonstrated that the biliproteins are physically attached to the photosystem II complexes, transferring light energy to the photosystem II reaction center chlorophyll d with high efficiency.  (+info)

Swimming marine Synechococcus strains with widely different photosynthetic pigment ratios form a monophyletic group. (7/197)

Unicellular marine cyanobacteria are ubiquitous in both coastal and oligotrophic regimes. The contribution of these organisms to primary production and nutrient cycling is substantial on a global scale. Natural populations of marine Synechococcus strains include multiple genetic lineages, but the link, if any, between unique phenotypic traits and specific genetic groups is still not understood. We studied the genetic diversity (as determined by the DNA-dependent RNA polymerase rpoC1 gene sequence) of a set of marine Synechococcus isolates that are able to swim. Our results show that these isolates form a monophyletic group. This finding represents the first example of correspondence between a physiological trait and a phylogenetic group in marine Synechococcus. In contrast, the phycourobilin (PUB)/phycoerythrobilin (PEB) pigment ratios of members of the motile clade varied considerably. An isolate obtained from the California Current (strain CC9703) displayed a pigment signature identical to that of nonmotile strain WH7803, which is considered a model for low-PUB/PEB-ratio strains, whereas several motile strains had higher PUB/PEB ratios than strain WH8103, which is considered a model for high-PUB/PEB-ratio strains. These findings indicate that the PUB/PEB pigment ratio is not a useful characteristic for defining phylogenetic groups of marine Synechococcus strains.  (+info)

Modification of intensity and direction of electron flow across bileaflet membranes. (8/197)

The intensity and the direction of electron flow across chloroplast extract bilayer membranes are modified by the presence of biliproteins. Biliproteins including C-phycocyanin, phycoerythrin, allophycocyanin, and Chroomonas phycocyanin enhance the photosensitivity of the membranes. The photoelectric spectra of the membranes in the presence of biliproteins correlate with the absorption spectra of these biliproteins. Experiments are presented to demonstrate the specific character of the electron-directing ability of biliproteins. A possible mechanism involving the interaction between the biliproteins and the membranes is proposed.  (+info)

Phycoerythrin is not a medical term, but a term used in biochemistry and cell biology. It refers to a type of protein found in certain algae and cyanobacteria that binds phycobilins, which are linear tetrapyrrole chromophores. Phycoerythrin is a light-harvesting pigment that absorbs light energy and transfers it to the photosynthetic reaction centers. It is often used in research and clinical settings as a fluorescent label for various applications, such as flow cytometry, immunohistochemistry, and microscopy.

Phycobilisomes are large, complex pigment-protein structures found in the thylakoid membranes of cyanobacteria and the chloroplasts of red algae and glaucophytes. They function as light-harvesting antennae, capturing light energy and transferring it to the photosynthetic reaction centers. Phycobilisomes are composed of phycobiliproteins, which are bound together in a highly organized manner to form rod-like structures called phycobil rods. These rods are attached to a central core structure called the phycobilisome core. The different types of phycobiliproteins absorb light at different wavelengths, allowing the organism to efficiently utilize available sunlight for photosynthesis.

Phycocyanin is a pigment-protein complex found in cyanobacteria and some types of algae, such as Spirulina. It belongs to the family of phycobiliproteins and plays a crucial role in the light-harvesting process during photosynthesis. Phycocyanin absorbs light in the orange and red regions of the visible spectrum and transfers the energy to chlorophyll for use in photosynthesis. It has been studied for its potential health benefits, including antioxidant, anti-inflammatory, and neuroprotective properties. However, more research is needed to fully understand its effects and potential therapeutic uses.

Bile pigments are the yellow-brown colored end products of hemoglobin breakdown in the liver. Hemoglobin is a protein found in red blood cells that carries oxygen throughout the body. When these cells are broken down, heme (the non-protein part of hemoglobin) is converted into biliverdin, which is then converted into bilirubin. Bilirubin is further metabolized and excreted by the liver as a component of bile, a digestive fluid that helps break down fats in the small intestine.

Under normal conditions, the liver effectively removes and excretes bilirubin from the body through the bile ducts into the small intestine. However, when there is an overproduction of bilirubin or a problem with its elimination, it can accumulate in the blood, leading to jaundice (yellowing of the skin and eyes) and other symptoms associated with liver dysfunction.

In summary, bile pigments are the waste products formed during the breakdown of hemoglobin, primarily consisting of bilirubin, which is eliminated from the body via the liver and bile ducts.

Biological pigments are substances produced by living organisms that absorb certain wavelengths of light and reflect others, resulting in the perception of color. These pigments play crucial roles in various biological processes such as photosynthesis, vision, and protection against harmful radiation. Some examples of biological pigments include melanin, hemoglobin, chlorophyll, carotenoids, and flavonoids.

Melanin is a pigment responsible for the color of skin, hair, and eyes in animals, including humans. Hemoglobin is a protein found in red blood cells that contains a porphyrin ring with an iron atom at its center, which gives blood its red color and facilitates oxygen transport. Chlorophyll is a green pigment found in plants, algae, and some bacteria that absorbs light during photosynthesis to convert carbon dioxide and water into glucose and oxygen. Carotenoids are orange, yellow, or red pigments found in fruits, vegetables, and some animals that protect against oxidative stress and help maintain membrane fluidity. Flavonoids are a class of plant pigments with antioxidant properties that have been linked to various health benefits.

Phycobilins are linear tetrapyrrole chromophores found in cyanobacteria, red algae, and glaucophytes. They are the light-harvesting pigments associated with phycobiliproteins in the phycobilisome complex, which is a type of antenna system used to capture light for photosynthesis. The main types of phycobilins are phycocyanobilin, phycoerythrobilin, and allophycocyanobilin. These pigments absorb light in the blue-green to red region of the electromagnetic spectrum and transfer the energy to chlorophyll a for use in photosynthesis. Phycobilins are also used as fluorescent labels in various biochemical and medical research applications.

Cyanobacteria, also known as blue-green algae, are a type of bacteria that obtain their energy through photosynthesis, similar to plants. They can produce oxygen and contain chlorophyll a, which gives them a greenish color. Some species of cyanobacteria can produce toxins that can be harmful to humans and animals if ingested or inhaled. They are found in various aquatic environments such as freshwater lakes, ponds, and oceans, as well as in damp soil and on rocks. Cyanobacteria are important contributors to the Earth's oxygen-rich atmosphere and play a significant role in the global carbon cycle.

Rhodophyta, also known as red algae, is a division of simple, multicellular and complex marine algae. These organisms are characterized by their red pigmentation due to the presence of phycobiliproteins, specifically R-phycoerythrin and phycocyanin. They lack flagella and centrioles at any stage of their life cycle. The cell walls of Rhodophyta contain cellulose and various sulphated polysaccharides. Some species have calcium carbonate deposits in their cell walls, which contribute to the formation of coral reefs. Reproduction in these organisms is typically alternation of generations with a dominant gametophyte generation. They are an important source of food for many marine animals and have commercial value as well, particularly for the production of agar, carrageenan, and other products used in the food, pharmaceutical, and cosmetic industries.

"Porphyria" is not a term that refers to a specific medical condition related to a particular organ or system. Instead, it is a group of disorders caused by abnormalities in the production of heme, a component of hemoglobin in red blood cells. Heme is synthesized through a series of chemical reactions known as the heme biosynthetic pathway.

Porphyrias are classified into two main types: acute and cutaneous. Acute porphyrias are characterized by neurological symptoms such as abdominal pain, muscle weakness, and psychiatric disturbances. Cutaneous porphyrias, on the other hand, primarily affect the skin, causing photosensitivity, blistering, and scarring.

The term "Porphyria" comes from the name of a genus of algae called Porphyra, which contains porphyrins, the same molecules that accumulate in people with porphyria. However, there is no direct relationship between the algae and the disease.

Light-harvesting protein complexes are specialized structures in photosynthetic organisms, such as plants, algae, and some bacteria, that capture and transfer light energy to the reaction centers where the initial chemical reactions of photosynthesis occur. These complexes consist of proteins and pigments (primarily chlorophylls and carotenoids) arranged in a way that allows them to absorb light most efficiently. The absorbed light energy is then converted into electrical charges, which are transferred to the reaction centers for further chemical reactions leading to the production of organic compounds and oxygen. The light-harvesting protein complexes play a crucial role in initiating the process of photosynthesis and optimizing its efficiency by capturing and distributing light energy.

Tetrapyrroles are a class of organic compounds that contain four pyrrole rings joined together in a macrocyclic structure. They are important in biology because they form the core structure of many essential cofactors and prosthetic groups in proteins, including heme, chlorophyll, and cobalamin (vitamin B12).

Heme is a tetrapyrrole that contains iron and is a crucial component of hemoglobin, the protein responsible for oxygen transport in red blood cells. Chlorophyll is another tetrapyrrole that contains magnesium and plays a vital role in photosynthesis, the process by which plants convert light energy into chemical energy. Cobalamin contains cobalt and is essential for DNA synthesis, fatty acid metabolism, and neurotransmitter synthesis.

Abnormalities in tetrapyrrole biosynthesis can lead to various diseases, such as porphyrias, which are characterized by the accumulation of toxic intermediates in the heme biosynthetic pathway.

Eukaryota is a domain that consists of organisms whose cells have a true nucleus and complex organelles. This domain includes animals, plants, fungi, and protists. The term "eukaryote" comes from the Greek words "eu," meaning true or good, and "karyon," meaning nut or kernel. In eukaryotic cells, the genetic material is housed within a membrane-bound nucleus, and the DNA is organized into chromosomes. This is in contrast to prokaryotic cells, which do not have a true nucleus and have their genetic material dispersed throughout the cytoplasm.

Eukaryotic cells are generally larger and more complex than prokaryotic cells. They have many different organelles, including mitochondria, chloroplasts, endoplasmic reticulum, and Golgi apparatus, that perform specific functions to support the cell's metabolism and survival. Eukaryotic cells also have a cytoskeleton made up of microtubules, actin filaments, and intermediate filaments, which provide structure and shape to the cell and allow for movement of organelles and other cellular components.

Eukaryotes are diverse and can be found in many different environments, ranging from single-celled organisms that live in water or soil to multicellular organisms that live on land or in aquatic habitats. Some eukaryotes are unicellular, meaning they consist of a single cell, while others are multicellular, meaning they consist of many cells that work together to form tissues and organs.

In summary, Eukaryota is a domain of organisms whose cells have a true nucleus and complex organelles. This domain includes animals, plants, fungi, and protists, and the eukaryotic cells are generally larger and more complex than prokaryotic cells.

Cryptophyta is a taxonomic division that refers to a group of unicellular algae called cryptomonads. These organisms are characterized by the presence of unique organelles called ejectisomes, which they use for defense and prey capture. They are also known for having two flagella and distinctive eyespot structures. Cryptophytes are widely distributed in aquatic environments and can be found in both freshwater and marine habitats. Some species are capable of carrying out photosynthesis, while others are heterotrophic, obtaining nutrients by consuming other organisms. The study of cryptomonads is important for understanding the evolution of eukaryotic cells and their complex organelles.

In the context of medical terminology, "light" doesn't have a specific or standardized definition on its own. However, it can be used in various medical terms and phrases. For example, it could refer to:

1. Visible light: The range of electromagnetic radiation that can be detected by the human eye, typically between wavelengths of 400-700 nanometers. This is relevant in fields such as ophthalmology and optometry.
2. Therapeutic use of light: In some therapies, light is used to treat certain conditions. An example is phototherapy, which uses various wavelengths of ultraviolet (UV) or visible light for conditions like newborn jaundice, skin disorders, or seasonal affective disorder.
3. Light anesthesia: A state of reduced consciousness in which the patient remains responsive to verbal commands and physical stimulation. This is different from general anesthesia where the patient is completely unconscious.
4. Pain relief using light: Certain devices like transcutaneous electrical nerve stimulation (TENS) units have a 'light' setting, indicating lower intensity or frequency of electrical impulses used for pain management.

Without more context, it's hard to provide a precise medical definition of 'light'.

Phycobiliproteins are pigment-protein complexes that are found in cyanobacteria (blue-green algae) and certain types of red algae. They are a part of the phycobilisome, a light-harvesting antenna complex located in the thylakoid membrane of these organisms. Phycobiliproteins play a crucial role in photosynthesis by capturing light energy and transferring it to chlorophylls for conversion into chemical energy.

There are three main types of phycobiliproteins:

1. Phycocyanin: This blue-colored pigment is responsible for the blue-green color of cyanobacteria. It absorbs light in the orange and red regions of the spectrum and emits fluorescence in the green region.
2. Phycoerythrin: This pink or red-colored pigment absorbs light in the blue and green regions of the spectrum and emits fluorescence in the orange and red regions. It is found in both cyanobacteria and red algae.
3. Allophycocyanin: This blue-green pigment absorbs light in the yellow and orange regions of the spectrum and emits fluorescence in the red region. It is found in cyanobacteria and some types of red algae.

Phycobiliproteins have been studied for their potential applications in various fields, including biotechnology, food technology, and medicine. For example, they are used as natural food colorants, fluorescent markers in research and diagnostics, and nutritional supplements with antioxidant properties.

"Plant proteins" refer to the proteins that are derived from plant sources. These can include proteins from legumes such as beans, lentils, and peas, as well as proteins from grains like wheat, rice, and corn. Other sources of plant proteins include nuts, seeds, and vegetables.

Plant proteins are made up of individual amino acids, which are the building blocks of protein. While animal-based proteins typically contain all of the essential amino acids that the body needs to function properly, many plant-based proteins may be lacking in one or more of these essential amino acids. However, by consuming a variety of plant-based foods throughout the day, it is possible to get all of the essential amino acids that the body needs from plant sources alone.

Plant proteins are often lower in calories and saturated fat than animal proteins, making them a popular choice for those following a vegetarian or vegan diet, as well as those looking to maintain a healthy weight or reduce their risk of chronic diseases such as heart disease and cancer. Additionally, plant proteins have been shown to have a number of health benefits, including improving gut health, reducing inflammation, and supporting muscle growth and repair.

Phycoerythrin (PE, λA max = 540-570 nm; λF max = 575-590 nm) R-Phycoerythrin and B-phycoerythrin are among the brightest ... B-phycoerythrin (B-PE) and R-phycoerythrin (R-PE) from red algae in addition to α and β chains have a third, γ subunit ... B-Phycoerythrin may also be less "sticky" than R-phycoerythrin and contributes less to background signal due to nonspecific ... "R-phycoerythrin (R-PE) - US". www.thermofisher.com. Retrieved 2021-12-11. Phycoerythrin at the U.S. National Library of ...
SH-Reactive R-Phycoerythrin ・Reducing Agent ・WS Buffer ・RA Solution 3 tubes. 3 tubes. 4 ml x 1. 1 ml x 1. 200μlx 1. 3 tubes. ... R-phycoerythrin Labeling Kit-SH is for simple and rapid preparation of R-PE-labeled IgG (Fig. 2). SH-reactive R-PE (a component ... R-phycoerythrin (R-PE) is one of the phycobiliproteins and has an orange fluorescence at around 578 nm, and it can be excited ... IgG or R-Phycoerythrin-conjugated IgG is always on the membrane of the filtration tube during the labeling process.. ♦ If the ...
Ab-10 Rapid R-Phycoerythrin Labeling Kit is for labeling R-Phycoerythrin to 10 µg antibody in less than 30 minutes. Labeling ... a) R-Phycoerythrin labeled-mouse anti-CD13 antibody. b) R-Phycoerythrin labeled-mouse antibody (Isotype) ... Reactive R-Phycoerythrin. ・Reaction Buffer. ・Stop Solution. ×3. 100μl×1. 100μl×1. ... 4 Staining HL60 cells with R-Phycoerythrin labeled antibody. ... Ab-10 Rapid R-Phycoerythrin Labeling Kit. Menu. *Description. * ...
The microalgal pigment phycoerythrin (PE) is of commercial interest as natural colorant in food and cosmetics, as well as ... A simple and fast method for extraction and quantification of cryptophyte phycoerythrin. I: MethodsX. 2017 ; Bind 4, Nr. C. s. ... A simple and fast method for extraction and quantification of cryptophyte phycoerythrin. MethodsX. 2017 jul. 28;4(C):209-213. ... N2 - The microalgal pigment phycoerythrin (PE) is of commercial interest as natural colorant in food and cosmetics, as well as ...
Anti-FSHR Mouse Monoclonal Antibody (PE (Phycoerythrin)) [clone: 626717]. Supplier: R & D Systems ...
Specific binding was evaluated by Phycoerythrin fluorescent labeling of R1EGO mouse thymoma cells. ...
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Anti Phycoerythrin Antibody is a highly pure affinity-purified polyclonal antibody specific to phycoerythrin (PE). This product ... Anti Phycoerythrin Antibody. $1,850.00. $1,150.00. Catalog Number: B2010809 (1 mg). Anti Phycoerythrin Antibody is a highly ... Anti Phycoerythrin Antibody. Catalog number: B2010809. Lot number: Batch Dependent. Expiration Date: Batch dependent. Amount: 1 ... R-phycoerythrin-conjugated antibodies are inappropriate for intracellular staining of murine plasma cells Cytometry A. 2013 May ...
Antibody Phycoerythrin Conjugated - 712-108-002 for WB. Reacts with Rat. Order online now! ... Related products to: F(ab)2 Rat IgG (H&L) Antibody Phycoerythrin conjugated. F(ab)2 Rat IgG (H&L) Antibody Fluorescein ... F(ab)2 Anti-Rat IgG Phycoerythrin Conjugated Antibody has been tested by western blot and is ideal for ELISA, western blotting ... Goat F(ab)2 Anti-Rat IgG Phycoerythrin Conjugated Antibody, Goat Fab2 Anti-Rat IgG Antibody PE Conjugation ...
Streptavidin, B-Phycoerythrin conjugated is produced as the B-phycoerythrin derivative of streptavidin and is provided in 0.1 M ... Streptavidin-B-Phycoerythrin (B-PE) can be used to label biotinylated proteins/antibodies and biotin derivatized surfaces ias ... Excess protein is removed by washing, and detection is mediated by adding Streptavidin-B-Phycoerythrin.The concentration ... Be the first to review "Streptavidin, B-Phycoerythrin conjugated" Cancel reply. Your rating. Rate…. Perfect. Good. Average. Not ...
C-phycoerythrin production from Anabaena sp. BTA 903: Optimization, production kinetics, thermodynam.... April 2023 · Biomass ... The yields of C-phycoerythrin, C-phycocyanin, allophycocyanin, chlorophyll-a, and ammonia excretion after 30 days of incubation ... cell growth along with C-phycoerythrin (PE) production. The light intensity of 6 k Lux, along with a photoperiod of 14:10 (L:D ...
View Mouse EphB2 Biotinylated Antibody (BAF467) datasheet.
查看 Human TrkB Biotinylated Antibody (BAF397) 数据表.
R-Phycoerythrin Amax: 488 Emax: 580nm Phycoerythrin (R-PE) is among several kinds of light-harvesting phycobiliproteins found ... R-Phycoerythrin AffiniPure F(ab)₂ Fragment Donkey Anti-Mouse IgG (H+L). (min X Bov, Ck, Gt, GP, Sy Hms, Hrs, Hu, Rb, Shp Sr ... Conjugate: R-Phycoerythrin Product Category: Fluorescent Protein Conjugates (R-PE, APC, and PerCP). Clonality: Polyclonal RRID: ... R-Phycoerythrin is licensed under U.S. Patents 4,5220,110 and 4,542,104; E.P.O. Patent 0076695; and Canadian Patent 1179942. ...
Fluorochromes: BV, brilliant violet; Cy, cyanine dye; PE, R-phycoerythrin; PerCP, peridinin-chlorophyll protein. ...
Antibody Phycoerythrin conjugated Min X Bv Hs & Hu Serum Proteins - 710-1822, Cellular Assay. Reacts with Mouse. Order online ... Related products to: F(ab)2 Mouse IgG F(c) Antibody Phycoerythrin Conjugated Pre-Adsorbed. F(ab)2 Mouse IgG (H&L) Antibody ... F(ab)2 Anti-Mouse IgG F(c) Phycoerythrin Antibody was generated in goat and detects specifically Mouse IgG F(c). Secondary ... Goat F(ab)2 Anti-Mouse IgG F(c) Antibody Phycoerythrin Conjugation, Goat Fab2 Anti-Mouse IgG Fc PE Conjugated Antibody ...
Whilst PBS genes in marine Synechococcus are mostly found in one type of phycoerythrin (PE) rich gene cluster (Type III), ... We detected a type II phycobilisome (PBS) gene cluster in both genomes, which suggests that they belong to a phycoerythrin-rich ... Whilst PBS genes in marine Synechococcus are mostly found in one type of phycoerythrin (PE) rich gene cluster (Type III), ... Insights Into the Evolution of Picocyanobacteria and Phycoerythrin Genes (mpeBA and cpeBA).. Ontology highlight ...
SMCC Activated B-PE (B-Phycoerythrin) - 1 mg *Cat.Number : AS-72109 ... SMCC Activated R-PE (R-Phycoerythrin) - 1 mg *Cat.Number : AS-72110 ...
Streptavidin, B-phycoerythrin conjugated - 0.5 mg *Cat.Number : AS-60662. Quick view ...
FITC, fluorescein isothiocyanate; PE, phycoerythrin.. Main Article. 1Preliminary findings from this study were presented at the ...
melting point of R-phycoerythrin Hello, please tell me if you know, what are melting point of R-phycoerythrin.. Thank you! ...
Limited by the dataset, the estimation of other pigment concentrations (phycoerythrin, chlorophyll b and c, carotenoids) from a ... phycoerythrin: 548.8 nm; and phycocyanin: 617.6 nm. These peak locations and widths (the second and third columns of Table 2) ...
While this was formerly attributed to the presence of pigments (such as phycoerythrin) that would permit red algae to inhabit ... Red algae are red due to phycoerythrin. They contain the sulfated polysaccharide carrageenan in the amorphous sections of their ... "Properties and Ultrastructure of Phycoerythrin From Porphyridium cruentum12". Plant Physiology. 44 (11): 1629-1638. doi ...
R-Phycoerythrin. 0 out of 5. $0.00. Read more Add to wishlist ...
SMCC Activated B-PE (B-Phycoerythrin) - 1 mg *Cat.Number : AS-72109 ... SMCC Activated R-PE (R-Phycoerythrin) - 1 mg *Cat.Number : AS-72110 ...
... phycoerythrin; MARCO, macrophage receptor with collagenous structure; PMA, phorbol 12-myristate 13-acetate; Poly(I:C), ...
R-Phycoerythrin-conjugated AffiniPure Fab Fragment Goat Anti-Human IgM, Fc5μ Fragment Specific」。富士フイルム和光純薬株式会社は、試験研究用試薬・抗体の製 ... R-Phycoerythrin-conjugated AffiniPure Fab Fragment Goat Anti-Human IgM, Fc5μ Fragment Specific R-Phycoerythrin-conjugated ... R-Phycoerythrin-conjugated AffiniPure Fab Fragment Goat Anti-Mouse IgM, μ Chain Specific ... R-Phycoerythrin-conjugated AffiniPure Fab Fragment Goat Anti-Human
R-Phycoerythrin/Cyanine 5 (2) * R-Phycoerythrin/Cyanine 7 (2) * R-phycoerythrin-Texas Red (1) ...
phycoerythrin. RLU. relative light units. RT. reverse transcription. SP1. specificity protein 1. TAM. tamoxifen. TCDD. 2,3,7,8- ...

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