A proteolytic enzyme obtained from Carica papaya. It is also the name used for a purified mixture of papain and CHYMOPAPAIN that is used as a topical enzymatic debriding agent. EC 3.4.22.2.
A sulfhydryl proteinase with cysteine at the active site from ficus latex. Preferential cleavage is at tyrosine and phenylalanine residues. EC 3.4.22.3.
A homologous group of endogenous CYSTEINE PROTEINASE INHIBITORS. The cystatins inhibit most CYSTEINE ENDOPEPTIDASES such as PAPAIN, and other peptidases which have a sulfhydryl group at the active site.
A cysteine endopeptidase isolated from papaya latex. Preferential cleavage at glutamic and aspartic acid residues. EC 3.4.22.6.
ENDOPEPTIDASES which have a cysteine involved in the catalytic process. This group of enzymes is inactivated by CYSTEINE PROTEINASE INHIBITORS such as CYSTATINS and SULFHYDRYL REAGENTS.
Protein-digesting and milk-clotting enzymes found in PINEAPPLE fruit juice and stem tissue. Enzymes from the two sources are distinguished as fruit bromelain and stem bromelain. This enzyme was formerly listed as EC 3.4.22.4.
A group of lysosomal proteinases or endopeptidases found in aqueous extracts of a variety of animal tissues. They function optimally within an acidic pH range. The cathepsins occur as a variety of enzyme subtypes including SERINE PROTEASES; ASPARTIC PROTEINASES; and CYSTEINE PROTEASES.
An ubiquitously-expressed lysosomal cysteine protease that is involved in protein processing. The enzyme has both endopeptidase and aminopeptidase activities.
A ubiquitously-expressed cysteine protease that plays an enzymatic role in POST-TRANSLATIONAL PROTEIN PROCESSING of proteins within SECRETORY GRANULES.
A lysosomal cysteine proteinase with a specificity similar to that of PAPAIN. The enzyme is present in a variety of tissues and is important in many physiological and pathological processes. In pathology, cathepsin B has been found to be involved in DEMYELINATION; EMPHYSEMA; RHEUMATOID ARTHRITIS, and NEOPLASM INVASIVENESS.
A reagent used for the determination of iron.
Exogenous and endogenous compounds which inhibit CYSTEINE ENDOPEPTIDASES.
A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.
An intracellular cystatin subtype that is found in a broad variety of cell types. It is a cytosolic enzyme inhibitor that protects the cell against the proteolytic action of lysosomal enzymes such as CATHEPSINS.
The rate dynamics in chemical or physical systems.
A plant genus of the family Caricaceae, order Violales, subclass Dilleniidae, class Magnoliopsida. It is the source of edible fruit and PAPAIN.
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)
A plant family of the order Violales, subclass Dilleniidae, class Magnoliopsida.
A serine protease that catalyses the release of an N-terminal dipeptide. Several biologically-active peptides have been identified as dipeptidyl peptidase 4 substrates including INCRETINS; NEUROPEPTIDES; and CHEMOKINES. The protein is also found bound to ADENOSINE DEAMINASE on the T-CELL surface and is believed to play a role in T-cell activation.

Expression of murine coronavirus recombinant papain-like proteinase: efficient cleavage is dependent on the lengths of both the substrate and the proteinase polypeptides. (1/976)

Proteolytic processing of the replicase gene product of mouse hepatitis virus (MHV) is essential for viral replication. In MHV strain A59 (MHV-A59), the replicase gene encodes two predicted papain-like proteinase (PLP) domains, PLP-1 and PLP-2. Previous work using viral polypeptide substrates synthesized by in vitro transcription and translation from the replicase gene demonstrated both cis and trans cleavage activities for PLP-1. We have cloned and overexpressed the PLP-1 domain in Escherichia coli by using a T7 RNA polymerase promoter system or as a maltose-binding protein (MBP) fusion protein. With both overexpression systems, the recombinant PLP-1 exhibited trans cleavage activity when incubated with in vitro-synthesized viral polypeptide substrates. Subsequent characterization of the recombinant PLP-1 revealed that in vitro trans cleavage is more efficient at 22 degrees C than at higher temperatures. Using substrates of increasing lengths, we observed efficient cleavage by PLP-1 requires a substrate greater than 69 kDa. In addition, when PLP-1 was expressed as a polypeptide that included additional viral sequences at the carboxyl terminus of the predicted PLP-1 domain, a fivefold increase in proteolytic activity was observed. The data presented here support previous data suggesting that in vitro and in vivo cleavage of the ORF 1a polyprotein by PLP-1 can occur in both in cis and in trans. In contrast to the cleavage activity demonstrated for PLP-1, no in vitro cleavage in cis or in trans could be detected with PLP-2 expressed either as a polypeptide, including flanking viral sequences, or as an MBP fusion enzyme.  (+info)

Expression and characterization of a DNase I-Fc fusion enzyme. (2/976)

Recombinant human deoxyribonuclease I (DNase I) is an important clinical agent that is inhaled into the airways where it degrades DNA to lower molecular weight fragments, thus reducing the viscoelasticity of sputum and improving the lung function of cystic fibrosis patients. To investigate DNases with potentially improved properties, we constructed a molecular fusion of human DNase I with the hinge and Fc region of human IgG1 heavy chain, creating a DNase I-Fc fusion protein. Infection of Sf9 insect cells with recombinant baculovirus resulted in the expression and secretion of the DNase I-Fc fusion protein. The fusion protein was purified from the culture medium using protein A affinity chromatography followed by desalting by gel filtration and was characterized by amino-terminal sequence, amino acid composition, and a variety of enzyme-linked immunosorbent assays (ELISA) and activity assays. The purified fusion contains DNase I, as determined by a DNase I ELISA and an actin-binding ELISA, and an intact antibody Fc region, which was quantified by an Fc ELISA, in a 2:1 stoichiometric ratio, respectively. The dimeric DNase I-Fc fusion was functionally active in enzymatic DNA digestion assays, albeit about 10-fold less than monomeric DNase I. Cleavage of the DNase I-Fc fusion by papain resulted in a specific activity comparable to the monomeric enzyme. Salt was inhibitory for wild type monomeric DNase I but actually enhanced the activity of the dimeric DNase I-Fc fusion. The DNase I-Fc fusion protein was also less Ca2+-dependent than DNase I itself. These results are consistent with a higher affinity of the dimeric fusion protein to DNA than monomeric DNase I. The engineered DNase I-Fc fusion protein described herein has properties that may have clinical benefits.  (+info)

Revisiting the S2 specificity of papain by structural analogs of Phe. (3/976)

Papain characteristically has a strong preference for encoded L-aromatic amino acids (Phe > Tyr) at P2 position. We re-examined papain S2 specificity using structural analogs of Phe, in fluorogenic substrates of the series: dansyl-Xaa-Arg-Ala-Pro-Trp (Xaa = P2 residue). Kinetic analyses showed that the S2 pocket accommodates a broad spectrum of Phe derivatives. Papain is poorly stereoselective towards Dns-(D/L)-Phe-Arg-Ala-Pro-Trp and binding is not critically affected by replacement of the benzyl ring by the non-aromatic lateral chain of cyclohexylalanine. The Km was significantly improved by mono- and di-chlorination of Phe, or by its substitution by an electronegative group-like NO2, but the specificity constant was unchanged. Shortening or lengthening the side chain by adding or removing a methylene group impairs the P2/S2 interactions significantly, as do constrained structural analogs of Phe. Incorporation of benzyl-substituted phenylalanyl amino acid could help to design peptide-derived inhibitors with greater affinity and bioavailability.  (+info)

A human RNA viral cysteine proteinase that depends upon a unique Zn2+-binding finger connecting the two domains of a papain-like fold . (4/976)

A cysteine proteinase, papain-like proteinase (PL1pro), of the human coronavirus 229E (HCoV) regulates the expression of the replicase polyproteins, pp1a and ppa1ab, by cleavage between Gly111 and Asn112, far upstream of its own catalytic residue Cys1054. In this report, using bioinformatics tools, we predict that, unlike its distant cellular homologues, HCoV PL1pro and its coronaviral relatives have a poorly conserved Zn2+ finger connecting the left and right hand domains of a papain-like fold. Optical emission spectrometry has been used to confirm the presence of Zn2+ in a purified and proteolytically active form of the HCoV PL1pro fused with the Escherichia coli maltose-binding protein. In denaturation/renaturation experiments using the recombinant protein, its activity was shown to be strongly dependent upon Zn2+, which could be partly substituted by Co2+ during renaturation. The reconstituted, Zn2+-containing PL1pro was not sensitive to 1,10-phenanthroline, and the Zn2+-depleted protein was not reactivated by adding Zn2+ after renaturation. Consistent with the proposed essential structural role of Zn2+, PL1pro was selectively inactivated by mutations in the Zn2+ finger, including replacements of any of four conserved Cys residues predicted to co-ordinate Zn2+. The unique domain organization of HCoV PL1pro provides a potential framework for regulatory processes and may be indicative of a nonproteolytic activity of this enzyme.  (+info)

Neutrophil elastase increases MUC5AC mRNA and protein expression in respiratory epithelial cells. (5/976)

Chronic neutrophil-predominant inflammation and hypersecretion of mucus are common pathophysiological features of cystic fibrosis, chronic bronchitis, and viral- or pollution-triggered asthma. Neutrophils release elastase, a serine protease, that causes increased mucin production and secretion. The molecular mechanisms of elastase-induced mucin production are unknown. We hypothesized that as part of this mechanism, elastase upregulates expression of a major respiratory mucin gene, MUC5AC. A549, a human lung carcinoma cell line that expresses MUC5AC mRNA and protein, and normal human bronchial epithelial cells in an air-liquid interface culture were stimulated with neutrophil elastase. Neutrophil elastase increased MUC5AC mRNA levels in a time-dependent manner in both cell culture systems. Neutrophil elastase treatment also increased MUC5AC protein levels in A549 cells. The mechanism of MUC5AC gene regulation by elastase was determined in A549 cells. The induction of MUC5AC gene expression required serine protease activity; other classes of proteases had no effect on MUC5AC gene expression. Neutrophil elastase increased MUC5AC mRNA levels by enhancing mRNA stability. This is the first report of mucin gene regulation by this mechanism.  (+info)

Collagen type I antisense and collagen type IIA messenger RNA is expressed in adult murine articular cartilage. (6/976)

OBJECTIVE: Articular cartilage has only limited capacities for repair and it is not known what is the exact mechanism of matrix restoration. It was investigated whether the reparative process in murine articular cartilage after moderate proteoglycan depletion is accompanied by a change in the chondrocyte phenotype either to hypertrophy or to a less differentiated phenotype as assayed by the expression of specific collagen subtypes. DESIGN: Moderate proteoglycan depletion was induced by injection of papain whereafter the expression of collagen type I mRNA, collagen IIA and IIB mRNA and type X collagen mRNA in patellar cartilage, as markers for chondrocyte phenotype, was investigated by RT-PCR during normal cartilage physiology and matrix restoration. In addition, in-situ expression of collagen subtypes was assayed by immunolocalisation. RESULTS: In normal articular cartilage collagen I, collagen IIB and collagen type X transcripts were easily detected. Surprisingly, collagen type I sense as well as antisense mRNA was detected and in addition to IIB transcripts collagen IIA transcripts were detected in a number of samples. During cartilage matrix restoration no change in the expression of collagen I, collagen IIA or IIB or collagen type X mRNA transcripts could be detected. Immunolocalization demonstrated the presence of type I (pericellular) and type II collagen in the extracellular matrix. The pericellular matrix of hypertrophic chondrocytes showed collagen type X staining in the calcified cartilage in normal and papain-injected knee joints. Increased staining for collagen type X was found in the upper cartilage layer in the interterritorial matrix from day 7 after papain injection. CONCLUSION: The absence of changes in collagen mRNA expression indicates that alteration of chondrocyte phenotype does not occur during the successful repair process after moderate proteoglycan depletion. Collagen type X appears to be deposited in the upper cartilage layer during this process.  (+info)

Binding modes of a new epoxysuccinyl-peptide inhibitor of cysteine proteases. Where and how do cysteine proteases express their selectivity? (7/976)

Papain from Carica papaya, an easily available cysteine protease, is the best-studied representative of this family of enzymes. The three dimensional structure of papain is very similar to that of other cysteine proteases of either plant (actinidin, caricain, papaya protease IV) or animal (cathepsins B, K, L, H) origin. As abnormalities in the activities of mammalian cysteine proteases accompany a variety of diseases, there has been a long-lasting interest in the development of potent and selective inhibitors for these enzymes. A covalent inhibitor of cysteine proteases, designed as a combination of epoxysuccinyl and peptide moieties, has been modeled in the catalytic pocket of papain. A number of its configurations have been generated and relaxed by constrained simulated annealing-molecular dynamics in water. A clear conformational variability of this inhibitor is discussed in the context of a conspicuous conformational diversity observed earlier in several solid-state structures of other complexes between cysteine proteases and covalent inhibitors. The catalytic pockets S2 and even more so S3, as defined by the pioneering studies on the papain-ZPACK, papain-E64c and papain-leupeptin complexes, appear elusive in view of the evident flexibility of the present inhibitor and in confrontation with the obvious conformational scatter seen in other examples. This predicts limited chances for the development of selective structure-based inhibitors of thiol proteases, designed to exploit the minute differences in the catalytic pockets of various members of this family. A simultaneous comparison of the three published proenzyme structures suggests the enzyme's prosegment binding loop-prosegment interface as a new potential target for selective inhibitors of papain-related thiol proteases.  (+info)

The affinity and kinetics of inhibition of cysteine proteinases by intact recombinant bovine cystatin C. (8/976)

Recent studies have shown that the bovine cysteine proteinase inhibitor, cystatin C, is synthesized as a preprotein containing a 118-residue mature protein. However, the forms of the inhibitor isolated previously from bovine tissues had shorter N-terminal regions than expected from these results, and also lower affinity for proteinases than human cystatin C. In this work, we report the properties of recombinant, full-length bovine cystatin C having a complete N-terminal region. The general characteristics of this form of the inhibitor, as reflected by the isoelectric point, the far-ultraviolet circular dichroism spectrum, the thermal stability and the changes of tryptophan fluorescence on interaction with papain, resembled those of human cystatin C. The affinity and kinetics of inhibition of papain and cathepsins B, H and L by the bovine inhibitor were also comparable with those of the human inhibitor, although certain differences were apparent. Notably, the affinity of bovine cystatin C for cathepsin H was somewhat weaker than that of human cystatin C, and bovine cystatin C bound to cathepsin L with about a four-fold higher association rate constant than the human inhibitor. This rate constant is comparable with the highest values reported previously for cystatin-cysteine proteinase reactions. The full-length, recombinant bovine cystatin C bound appreciably more tightly to proteinases than the shorter form characterized previously. Digestion of the recombinant inhibitor with neutrophil elastase resulted in forms with truncated N-terminal regions and appreciably decreased affinity for papain, consistent with the forms of bovine cystatin C isolated previously having arisen by proteolytic cleavage of a mature, full-length inhibitor.  (+info)

Papain is defined as a proteolytic enzyme that is derived from the latex of the papaya tree (Carica papaya). It has the ability to break down other proteins into smaller peptides or individual amino acids. Papain is widely used in various industries, including the food industry for tenderizing meat and brewing beer, as well as in the medical field for its digestive and anti-inflammatory properties.

In medicine, papain is sometimes used topically to help heal burns, wounds, and skin ulcers. It can also be taken orally to treat indigestion, parasitic infections, and other gastrointestinal disorders. However, its use as a medical treatment is not widely accepted and more research is needed to establish its safety and efficacy.

Ficain is not typically defined in the context of human medicine, but it is a term used in biochemistry and molecular biology. Ficain is a proteolytic enzyme, also known as ficin, that is isolated from the latex of the fig tree (Ficus species). It has the ability to break down other proteins into smaller peptides or individual amino acids by cleaving specific peptide bonds. Ficain is often used in research and industrial applications, such as protein degradation, digestion studies, and biochemical assays.

Cystatins are a group of proteins that inhibit cysteine proteases, which are enzymes that break down other proteins. Cystatins are found in various biological fluids and tissues, including tears, saliva, seminal plasma, and urine. They play an important role in regulating protein catabolism and protecting cells from excessive protease activity. There are three main types of cystatins: type 1 (cystatin C), type 2 (cystatin M, cystatin N, and fetuin), and type 3 (kininogens). Abnormal levels of cystatins have been associated with various pathological conditions, such as cancer, neurodegenerative diseases, and inflammatory disorders.

Chymopapain is a proteolytic enzyme that is derived from the papaya fruit (Carica papaya). It is specifically obtained from the latex of unripe papayas. Chymopapain is used in medical treatments, particularly as an enzyme therapy for disc herniation in the spine, which can cause pain, numbness, or weakness due to pressure on nearby nerves.

The procedure, called chemonucleolysis, involves injecting chymopapain directly into the damaged intervertebral disc. The enzyme breaks down and dissolves part of the proteoglycan matrix in the nucleus pulposus (the inner, gel-like portion of the intervertebral disc), reducing its size and relieving pressure on the affected nerves. This can help alleviate pain and improve function in some patients with herniated discs.

However, the use of chymopapain for disc herniation has declined over time due to the development of other treatment options, such as minimally invasive surgical techniques, and concerns about potential side effects and allergic reactions associated with its use. It is essential to consult a healthcare professional for appropriate evaluation and management of spinal conditions.

Cysteine endopeptidases are a type of enzymes that cleave peptide bonds within proteins. They are also known as cysteine proteases or cysteine proteinases. These enzymes contain a catalytic triad consisting of three amino acids: cysteine, histidine, and aspartate. The thiol group (-SH) of the cysteine residue acts as a nucleophile and attacks the carbonyl carbon of the peptide bond, leading to its cleavage.

Cysteine endopeptidases play important roles in various biological processes, including protein degradation, cell signaling, and inflammation. They are involved in many physiological and pathological conditions, such as apoptosis, immune response, and cancer. Some examples of cysteine endopeptidases include cathepsins, caspases, and calpains.

It is important to note that these enzymes require a reducing environment to maintain the reduced state of their active site cysteine residue. Therefore, they are sensitive to oxidizing agents and inhibitors that target the thiol group. Understanding the structure and function of cysteine endopeptidases is crucial for developing therapeutic strategies that target these enzymes in various diseases.

Bromelains are a group of enzymes found in pineapple plants, primarily in the stem and fruit. These enzymes have been studied for their potential medicinal properties, including anti-inflammatory, analgesic, and digestive benefits. Bromelains can help break down proteins, which may support digestion and reduce inflammation in the body. They have been used in complementary medicine to treat a variety of conditions, such as osteoarthritis, sinusitis, and post-surgical inflammation. However, more research is needed to fully understand their effectiveness and safety.

Cathepsins are a type of proteolytic enzymes, which are found in lysosomes and are responsible for breaking down proteins inside the cell. They are classified as papain-like cysteine proteases and play important roles in various physiological processes, including tissue remodeling, antigen presentation, and apoptosis (programmed cell death). There are several different types of cathepsins, including cathepsin B, C, D, F, H, K, L, S, V, and X/Z, each with distinct substrate specificities and functions.

Dysregulation of cathepsins has been implicated in various pathological conditions, such as cancer, neurodegenerative diseases, and inflammatory disorders. For example, overexpression or hyperactivation of certain cathepsins has been shown to contribute to tumor invasion and metastasis, while their inhibition has been explored as a potential therapeutic strategy in cancer treatment. Similarly, abnormal levels of cathepsins have been linked to the progression of neurodegenerative diseases like Alzheimer's and Parkinson's, making them attractive targets for drug development.

Cathepsin H is a lysosomal cysteine protease that plays a role in intracellular protein degradation and turnover. It is expressed in various tissues, including the spleen, thymus, lungs, and immune cells. Cathepsin H has been implicated in several physiological processes, such as antigen presentation, bone resorption, and extracellular matrix remodeling. Additionally, its dysregulation has been associated with various pathological conditions, including cancer, neurodegenerative disorders, and infectious diseases.

The enzyme's active site contains a catalytic triad composed of cysteine, histidine, and aspartic acid residues, which facilitates the proteolytic activity. Cathepsin H exhibits specificity for peptide bonds containing hydrophobic or aromatic amino acids, making it an important player in processing and degrading various cellular proteins.

In summary, Cathepsin H is a lysosomal cysteine protease involved in protein turnover and degradation with potential implications in several pathological conditions when dysregulated.

Cathepsin L is a lysosomal cysteine protease that plays a role in various physiological processes, including protein degradation, antigen presentation, and extracellular matrix remodeling. It is produced as an inactive precursor and activated by cleavage of its propeptide domain. Cathepsin L has a broad specificity for peptide bonds and can cleave both intracellular and extracellular proteins, making it an important player in various pathological conditions such as cancer, neurodegenerative diseases, and infectious diseases. Inhibition of cathepsin L has been explored as a potential therapeutic strategy for these conditions.

Cathepsin B is a lysosomal cysteine protease that plays a role in various physiological processes, including intracellular protein degradation, antigen presentation, and extracellular matrix remodeling. It is produced as an inactive precursor (procathepsin B) and activated upon cleavage of the propeptide by other proteases or autocatalytically. Cathepsin B has a wide range of substrates, including collagen, elastin, and various intracellular proteins. Its dysregulation has been implicated in several pathological conditions, such as cancer, neurodegenerative diseases, and inflammatory disorders.

'2,2'-Dipyridyl is an organic compound with the formula (C5H4N)2. It is a bidentate chelating ligand, which means that it can form stable coordination complexes with many metal ions by donating both of its nitrogen atoms to the metal. This ability to form complexes makes '2,2'-Dipyridyl useful in various applications, including as a catalyst in chemical reactions and as a reagent in the analysis of metal ions.

The compound is a solid at room temperature and has a molecular weight of 108.13 g/mol. It is soluble in organic solvents such as ethanol, acetone, and dichloromethane, but is insoluble in water. '2,2'-Dipyridyl is synthesized by the reaction of pyridine with formaldehyde and hydrochloric acid.

In medical contexts, '2,2'-Dipyridyl may be used as a reagent in diagnostic tests to detect the presence of certain metal ions in biological samples. However, it is not itself a drug or therapeutic agent.

Cysteine proteinase inhibitors are a type of molecule that bind to and inhibit the activity of cysteine proteases, which are enzymes that cleave proteins at specific sites containing the amino acid cysteine. These inhibitors play important roles in regulating various biological processes, including inflammation, immune response, and programmed cell death (apoptosis). They can also have potential therapeutic applications in diseases where excessive protease activity contributes to pathology, such as cancer, arthritis, and neurodegenerative disorders. Examples of cysteine proteinase inhibitors include cystatins, kininogens, and serpins.

Endopeptidases are a type of enzyme that breaks down proteins by cleaving peptide bonds inside the polypeptide chain. They are also known as proteinases or endoproteinases. These enzymes work within the interior of the protein molecule, cutting it at specific points along its length, as opposed to exopeptidases, which remove individual amino acids from the ends of the protein chain.

Endopeptidases play a crucial role in various biological processes, such as digestion, blood coagulation, and programmed cell death (apoptosis). They are classified based on their catalytic mechanism and the structure of their active site. Some examples of endopeptidase families include serine proteases, cysteine proteases, aspartic proteases, and metalloproteases.

It is important to note that while endopeptidases are essential for normal physiological functions, they can also contribute to disease processes when their activity is unregulated or misdirected. For instance, excessive endopeptidase activity has been implicated in the pathogenesis of neurodegenerative disorders, cancer, and inflammatory conditions.

Cystatin B is a type of protease inhibitor that belongs to the cystatin superfamily. It is primarily produced in the central nervous system and is found in various body fluids, including cerebrospinal fluid and urine. Cystatin B plays a crucial role in regulating protein catabolism by inhibiting lysosomal cysteine proteases, which are enzymes that break down proteins.

Defects or mutations in the gene that encodes for cystatin B have been associated with a rare inherited neurodegenerative disorder known as Uner Tan Syndrome (UTS). UTS is characterized by language impairment, mental retardation, and distinctive facial features. The exact mechanism by which cystatin B deficiency leads to this disorder is not fully understood, but it is thought to involve the dysregulation of protein catabolism in neurons, leading to neurotoxicity and neurodegeneration.

In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."

1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.

2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.

3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.

4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).

Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.

"Carica" is a genus name that refers to a group of plants commonly known as papayas. The most widely cultivated and well-known species in this genus is Carica papaya, which is native to Central America and southern Mexico. This plant produces large, edible fruits that are rich in nutrients such as vitamin C, vitamin A, and potassium.

The fruit of the Carica papaya tree is often used for its medicinal properties, including its anti-inflammatory and digestive benefits. The leaves, stems, and roots of the plant also have various traditional uses in different cultures, such as treating wounds, reducing fever, and alleviating symptoms of digestive disorders.

It's worth noting that while Carica papaya has been studied for its potential health benefits, more research is needed to fully understand its effects and safety profile. As with any treatment or supplement, it's important to consult with a healthcare provider before using Carica papaya for medicinal purposes.

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.

Caricaceae is a family of flowering plants that includes several genera and species, the most notable of which is probably *Carica papaya*, the papaya or pawpaw tree. It belongs to the order Brassicales, which contains other economically important plant families such as Brassicaceae (mustards and cabbages) and Capparaceae (caper family).

The plants in Caricaceae are primarily found in tropical regions of the Americas, with a few species occurring in Africa. They are characterized by their simple, alternate leaves and distinctive flowers, which often have five distinct sepals and petals. The fruits of these plants can vary widely in size, shape, and color, but they typically contain numerous small seeds.

In addition to papaya, other economically important species in Caricaceae include *Vasconcellea cundinamarcensis*, which is used for its starchy roots, and *Jacaratia spinosa*, whose fruit is eaten in some parts of South America.

Dipeptidyl peptidase 4 (DPP-4) is a serine protease enzyme that is widely distributed in various tissues and organs, including the kidney, liver, intestines, and immune cells. It plays a crucial role in regulating several biological processes, such as glucose metabolism, immune function, and cell signaling.

In terms of glucose metabolism, DPP-4 is responsible for breaking down incretin hormones, including glucagon-like peptide-1 (GLP-1) and glucose-dependent insulinotropic polypeptide (GIP), which are released from the gut in response to food intake. These hormones stimulate insulin secretion from pancreatic beta cells, suppress glucagon release, and promote satiety, thereby helping to regulate blood sugar levels. By degrading GLP-1 and GIP, DPP-4 reduces their activity and contributes to the development of type 2 diabetes.

DPP-4 inhibitors are a class of drugs used to treat type 2 diabetes by blocking the action of DPP-4 and increasing incretin hormone levels, leading to improved insulin secretion and glucose control.

... info on papin Papain Applications, Inhibitors and Substrates Data sheet-Papain from BIOZYM Papain on Proteopedia (wiki with ... Papain is added to some toothpastes and mint sweets as a tooth whitener. Its whitening effect is minimal, because the papain is ... Papain belongs to a family of related proteins, known as the papain-like protease family, with a wide variety of activities, ... Papain is a relatively heat-resistant enzyme, with an optimal temperature range of 60 to 70 °C. Papain prefers to cleave after ...
... s (or papain-like (cysteine) peptidases; abbreviated PLP or PLCP) are a large protein family of cysteine ... In the MEROPS protease enzyme classification system, papain-like proteases form Clan CA. Papain-like proteases share a common ... Papain-like proteases have a catalytic dyad consisting of a cysteine and a histidine residue, which form an ion pair through ... Although papain-like proteases are found in all domains of life, they have been less well-studied in prokaryotes than in ...
The nidoviral papain-like protease (PLPro or PLP) is a papain-like protease protein domain encoded in the genomes of ... nidoviral papain-like proteases are members of clan CA, the papain-like proteases, whose structures and catalytic mechanisms ... In coronaviruses, single papain-like protease domains are usually known as PLPro, as for example in SARS-CoV and SARS-CoV-2. ... Coronaviruses have one or two papain-like protease domains; in SARS-CoV and SARS-CoV-2, one PLPro domain is located in ...
... is an American law firm headquartered in New York City. It is noted for its work on ... "Sullivan Papain Block McGrath & Cannavo P.C. , Hackensack NJ Law , LawyerLand". www.lawyerland.com. Retrieved 2017-06-19. [1] ... Established over 75 years ago, Sullivan & Papain employs 39 lawyers in four offices, with its main office located in New York ...
Because the enzyme papain acts as an allergen in sensitive individuals, meat that has been tenderized with it may induce an ... "Papain". National Library of Medicine, US National Institutes of Health. 27 April 2019. Retrieved 29 April 2019. United States ... Papaya is not suitable for gelatin-based desserts because the enzymatic properties of papain prevent gelatin from setting. In ... Both green papaya fruit and its latex are rich in papain, a protease used for tenderizing meat and other proteins, as practiced ...
I. Papain". Biochem. Biophys. Res. Commun. 27 (2): 157-162. doi:10.1016/S0006-291X(67)80055-X. PMID 6035483. Persson E, Bak H, ...
I. Papain. Biochim. Biophys. Res. Commun, 27 (1967), pp. 157-162. Nakano M, Tobets T, et al. (1990). "Further fractionation of ...
Papain, Jessie. "Wicked ends on a high note". Yahoo!7. Archived from the original on March 19, 2016. Retrieved June 30, 2015. " ...
Martin, S. (1886). "Papain and Dyspepsia". British Medical Journal. 1 (1319): 716. doi:10.1136/bmj.1.1319.716. PMC 2256824. ...
Drenth J, Jansonius JN, Koekoek R, Swen HM, Wolthers BG (June 1968). "Structure of papain". Nature. 218 (5145): 929-32. Bibcode ... concept of the domain was first proposed in 1973 by Wetlaufer after X-ray crystallographic studies of hen lysozyme and papain ...
Along with papain, bromelain is one of the most popular proteases to use for meat tenderizing. Bromelain is sold in a powdered ... Phytochemicals Papain "Bromelain". PubChem, National Library of Medicine, US National Institutes of Health. 14 September 2019. ... and papain) has been investigated in Europe to evaluate the efficacy in breast, colorectal, and plasmacytoma cancer patients. ...
Papain EMBL-EBI, InterPro. "Peptidase C1A, papain C-terminal (IPR000668) < InterPro < EMBL-EBI". www.ebi.ac.uk. Retrieved 2018- ... "Peptidase C1A, papain C-terminal (IPR000668) < InterPro < EMBL-EBI". www.ebi.ac.uk. Retrieved 2018-10-20. Gariev, Igor A. "HCS ... "Study of the extraction process of papain from latex of papaya ( Carica papaya L . ) fruits cv . Maradol." (2013). Ebata M, ... The MEROPS online database for peptidases and their inhibitors: C01.002 Data sheet for Papain from BIOZYM Portal: Biology (CS1 ...
Vinegar and papain are ineffective.[citation needed] Weever Scorpion fish Stone fish Snake bite Skin lesion Findlay E. Russell ...
Papain, Jessie (17 November 2015). "Big T leaves The X Factor". The West Australian. Retrieved 20 November 2015. Roman, Nick ( ...
p. 3. Papain, Jessie (19 September 2014). "Judd pays tribute to Tarvydas". The West Australian. Davies, Claire; Uren, Kate. " ...
But it also has a really strong message to it, which I really connected with." Papain noted that the ballad "has an ethereal, ... Papain, Jessie (7 November 2014). "A Derry little Christmas". The West Australian. Seven West Media. Retrieved 23 December 2014 ... Papain, Jessie (10 December 2014). "London calling Reigan Derry". The West Australian. Seven West Media. Retrieved 23 December ... In an interview with Jessie Papain of The West Australian, Derry recalled the moment she first heard "All of the Pieces", ...
Papain, Jessie (19 September 2014). "Judd pays tribute to Tarvydas". The West Australian. Retrieved 21 September 2014. Fenner, ...
Papain, Jessie (28 September 2015). "Peacocke at home in Wanted role". The West Australian. Archived from the original on 30 ...
In 2005, Badillo became "of counsel" to the New York City law firm of Sullivan Papain Block McGrath & Cannavo P.C. In 2006 he ... "Of Counsel Profile: Badillo, Herman". Sullivan, Papain, Block, McGrath, & Cannavo. 2002. Archived from the original on October ...
Papain, Jessie (10 July 2014). "Reigan Derry auditions for The X Factor". The West Australian. Seven West Media. Retrieved 9 ...
Papain, Jessie (25 May 2015). "Perth Wildcat tamed by stunning bride". TheWest.com.au. Retrieved 16 May 2018. "Brisbane Bullets ...
Fab fragments are generated by cleavage of IgG with papain instead of pepsin. Papain cleaves IgG above the hinge region ... 3. Mapping the active site of papain; specific peptide inhibitors of papain". Biochemical and Biophysical Research ...
Papain, Jessie (28 September 2015). "Peacocke at home in Wanted role". The West Australian. Retrieved 30 October 2015. "The ...
Papain, Jessie (1 October 2014). "Nathaniel Willemse to support Mariah Carey". The West Australian. Seven West Media. Retrieved ...
Papain, Jessie (29 September 2018). "Heath Ledger Scholarship winner Charmaine Bingwa hunts down Oscar". The West Australian. ...
Papain, Jessie (5 September 2014). "Mum's OK with being the joke". Yahoo! News. Yahoo News. Archived from the original on 5 ...
Cause this ain't love that I feel." Jessie Papain of The West Australian described "This Ain't Love" as "synth-heavy". Several ... Papain, Jessie (21 September 2015). "Mauboy rocks the city". The West Australian. Retrieved 22 September 2015. "Jessica Mauboy ...
Polgár, L. (1979). "Deuterium isotope effects on papain acylation. Evidence for lack of general base catalysis and for enzyme- ...
Polgár L (August 1979). "Deuterium isotope effects on papain acylation. Evidence for lack of general base catalysis and for ...
Papain's long-lost cousin, phytochelatin synthase". Plant Physiol. 136 (1): 2463-2474. doi:10.1104/pp.104.048579. PMC 523314. ... Vivares, D.; Arnoux, P.; Pignol, D. (2005). "A papain-like enzyme at work: Native and acyl-enzyme intermediate structures in ... Rea, P.A. (2006). "Phytochelatin synthase, papain's cousin, in stereo". Proc. Natl. Acad. Sci. 103 (3): 507-508. Bibcode: ... "Mutagenic definition of papain-like catalytic triad, sufficiency of N-terminal domain for single-site core catalytic enzyme ...
... info on papin Papain Applications, Inhibitors and Substrates Data sheet-Papain from BIOZYM Papain on Proteopedia (wiki with ... Papain is added to some toothpastes and mint sweets as a tooth whitener. Its whitening effect is minimal, because the papain is ... Papain belongs to a family of related proteins, known as the papain-like protease family, with a wide variety of activities, ... Papain is a relatively heat-resistant enzyme, with an optimal temperature range of 60 to 70 °C. Papain prefers to cleave after ...
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Papain has wide specificity and it will degrade most protein substrates more extensively than the ... Papain is a sulfhydryl protease from Carica papaya latex. ... Dissociating Enzymes: Papain. Papain is a sulfhydryl protease ... Papain * Chymotrypsin * Deoxyribonuclease I * Neutral Protease (Dispase) * Trypsin Inhibitor (Soybean) * Animal Origin Free ( ... Papain has wide specificity and it will degrade most protein substrates more extensively than the pancreatic proteases. It also ...
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A new class of papain-like protease/deubiquitinase inhibitors blocks SARS virus replication ... A new class of papain-like protease/deubiquitinase inhibitors blocks SARS virus replication. Mesecar, A.D., Ratia, K., Pegan, S ... A new class of papain-like protease/deubiquitinase inhibitors blocks SARS virus replication. *PDB DOI: https://doi.org/10.2210/ ...
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Papain Market is expected to develop at a CAGR of 5.90%, reaching a valuation of $ 0.41 billion During the projected period of ... Thus, driving the Papain market revenue.. Papain Market Segment Insights. Papain Form Insights. Based on the form, the Papain ... Global Papain Market Overview. Papain Market Size was valued at USD 0.25 Billion in 2022. The Papain market industry is ... Papain Market Trends. * Growing health awareness is driving the market growth. Market CAGR for papain is being driven by rising ...
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Gao X, et al., Crystal structure of SARS-CoV-2 papain-like protease. Acta Pharm Sin B. 2021; 11: 237-245. DOI: 10.1016/j.apsb. ... Shin D. et al. Papain-like protease regulates SARS-CoV-2 viral spread and innate immunity. Nature 2020; 587, 657-662. DOI: ... Mielech A M, et al. MERS-CoV papain-like protease has deISGylating and deubiquitinating activities. Virology 2014; 450-451, 64- ... GuanQun L, et al., ISG15-dependent activation of the sensor MDA5 is antagonized by the SARS-CoV-2 papain-like protease to evade ...
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Group C: 10% papain (ORGANIKA, Canada) prepared by 10 g of papain powder in 100 mL distilled water was used for the dentin ... 10% papain 60 seconds + Clearfil SE bond + composite resin. Group D. 10% papain 60 seconds + 37% H3PO4, 15 seconds + Adper ... Group D: Dentin surface treatment with 10% papain was applied for 60 seconds with a microbrush. The papain was washed for 15 ... papain + Clearfil SE bond. (D) 10% papain + Adper single bond 2. (E) 6% bromelain + Clearfil SE bond. (F) 6% bromelain + Adper ...
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... The SARS-CoV-2 papain-like protease (PLpro) is a part of NSP3 multi-domain ... The designed SARS-CoV-2 Papain-like Protease Targeted Library comprises only drug-like compounds (PAINS compounds are filtered ... Home > PRODUCTS > Targeted Libraries > SARS-CoV-2 Targeted Libraries > SARS-CoV-2 Papain-like ProteaseTargeted Library ... We offer SARS-CoV-2 Papain-like Protease (PLpro) Targeted Library, which contains 1051 compounds with predicted activity ...
cathepsin L - C1: Papain. Detailed annotation on the structure, function, physiology, pharmacology and clinical relevance of ... C1: Papain: cathepsin L. Last modified on 26/08/2021. Accessed on 08/12/2023. IUPHAR/BPS Guide to PHARMACOLOGY, https://www. ...
Theppakorn, T. and Kanasawud, P. and Halling, P.J. (2003) Effect of solid-state buffers on the catalytic activity of papain in ... The catalytic activity of papain in the synthesis of Z-Gly-Phe- NH2 in tert-butanol has been studied in the presence of solid- ... Hence, at least these buffers do not seem to be able to affect the protonation state and catalytic activity of papain. In the ... papain, solid-state buffer, catalytic activity, low water media Organic-solvents, amino-acids, esterification, biocatalysis, ph ...
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Papain is an active component in powder form for meat tenderizers and has a huge demand in the global market. Papain also used ... Global papain market is segmented by end-use industry and by region. By end-use industry, the global papain market is sub- ... The North America papain market accounts for relatively high revenue share, followed by Western Europe papain market over the ... Papain Extraction From Papaya Papain is a natural cysteine proteolytic enzyme present in mountain papaya (Vasconcellea ...
Clan C1A or papain superfamily cysteine proteases are key players in many important physiological processes and diseases in ... papain and cathepsin L) was validated. Furthermore, molecular dynamics simulation of the Mco-CPI-papain complex validated the ... Clan C1A or papain superfamily cysteine proteases are key players in many important physiological processes and diseases in ... Repurposing the mcoti-ii rigid molecular scaffold in to inhibitor of papain superfamily cysteine proteases. Manasi Mishra ...
Sensitization and challenge of mice with Ovalbumin (OVA)-Alum and papain-OVA also showed normal expansion of Th2 responses, ... Sensitization and challenge of mice with Ovalbumin (OVA)-Alum and papain-OVA also showed normal expansion of Th2 responses, ...
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THE ESTIMATION OF PEPSIN, TRYPSIN, PAPAIN, AND CATHEPSIN WITH HEMOGLOBIN.. scientific article published on September 1938 ...
Scientists suggest targeting the SARS-CoV-2 papain-like protease (PLpro) with inhibitors could prevent the spread of infection. ... SARS-CoV-2 papain-like protease could be a novel drug target. 6 ... According to researchers, inhibiting the SARS-CoV-2 papain-like ... Scientists suggest targeting the SARS-CoV-2 papain-like protease (PLpro) with inhibitors could prevent the spread of infection. ...
Papain, Specification 60 TU/mg-1750 TU/mg; Standard Enterprise standard; CAS NO. 9001-73-4 ... Papain. Specification 60 TU/mg-1750 TU/mg; Standard Enterprise standard; CAS NO. 9001-73-4. ...
They are also known for their anti-inflammatory properties, the relieving of pain, caring for wounds and papain is even used ... The protein enzymes Papain and Bromelain present in papaya and pineapple have many health benefits to the body in addition to ... What are Papain and Bromelain?. Papain is an enzyme coming from the papaya fruit (Carica papaya) that is used in the breakdown ... Who should take Bromelain and Papain?. Though large amounts of Bromelain and Papain are not required for daily health, they are ...
  • Papain, also known as papaya proteinase I, is a cysteine protease (EC 3.4.22.2) enzyme present in papaya (Carica papaya) and mountain papaya (Vasconcellea cundinamarcensis). (wikipedia.org)
  • It is the namesake member of the papain-like protease family. (wikipedia.org)
  • Papain belongs to a family of related proteins, known as the papain-like protease family, with a wide variety of activities, including endopeptidases, aminopeptidases, dipeptidyl peptidases and enzymes with both exo- and endopeptidase activity. (wikipedia.org)
  • Papain is a sulfhydryl protease from Carica papaya latex. (worthington-biochem.com)
  • SARS-CoV-2 requires two cysteine proteases for viral polypeptide processing to allow maturation and replication: the 3C-like protease also known as the Main protease (M pro ) and the papain-like protease (PL pro ). (biorxiv.org)
  • The SARS-CoV-2 papain-like protease (PLpro) is a part of NSP3 multi-domain protein. (otavachemicals.com)
  • We offer SARS-CoV-2 Papain-like Protease (PLpro) Targeted Library , which contains 1051 compounds with predicted activity against this protease. (otavachemicals.com)
  • The designed SARS-CoV-2 Papain-like Protease Targeted Library comprises only drug-like compounds (PAINS compounds are filtered off). (otavachemicals.com)
  • Scientists suggest targeting the SARS-CoV-2 papain-like protease (PLpro) with inhibitors could prevent the spread of infection. (drugtargetreview.com)
  • According to researchers, inhibiting the SARS-CoV-2 papain-like protease (PLpro) could prevent viral replication and enhance the human immune response. (drugtargetreview.com)
  • Papain (EC=3.4.22.2) is a cysteine protease which belongs to peptidase C1 family. (agrisera.com)
  • Replication of severe acute respiratory syndrome (SARS) coronavirus (SARS-CoV) requires proteolytic processing of the replicase polyprotein by two viral cysteine proteases, a chymotrypsin-like protease (3CLpro) and a papain-like protease (PLpro). (novoprolabs.com)
  • Papaya has the highest concentration of protease (enzyme), Papain commonly used as a meat tenderiser. (hoptoitbunnies.com)
  • Sulfur Free Papain Powder is a kind of protease that derived from the papaya tree's fruit. (enzymeindia.co.in)
  • Some species have more than one papain-like protease gene. (bvsalud.org)
  • Potential COVID-19 papain-like protease PL inhibitors: repurposing FDA-approved drugs. (cdc.gov)
  • Food and beverages infused with papain enzymes aid digestion and can be used as a natural anti-inflammatory and for fluid retention following trauma or surgery. (marketresearchfuture.com)
  • The protein enzymes Papain and Bromelain present in papaya and pineapple have many health benefits to the body in addition to assisting in the breakdown of proteins during digestion. (oxfordvitality.co.uk)
  • Super Bromelain + Papain 90 tablets is an excellent combination of two proteolytic enzymes from pineapple and papaya. (alfafit.eu)
  • Papain is a natural biological enzyme preparation extracted from the unripe pulp of papaya through bioengineering technology, mainly composed of papain, papaya rennet A, papaya rennet B, papaya peptidase B and other proteolytic enzymes, which consists of 212 amino acids and has a molecular weight of 27000. (enzymes.bio)
  • There were no significant differences considering the specimens exposed to papain before the total etch adhesive system ( p = 0.13), and the specimens were exposed to bromelain enzyme before self-etch and total etch adhesive systems ( p = 0.25, p = 0.84, respectively). (thejcdp.com)
  • Additionally, the application of bromelain enzyme as dentin treatment before two adhesive systems and papain before total etch adhesive system had no effect on the SBS of composite to superficial dentin. (thejcdp.com)
  • Much like its cousin Bromelain, Papain also contains anti-inflammatory properties. (oxfordvitality.co.uk)
  • Who should take Bromelain and Papain? (oxfordvitality.co.uk)
  • Though large amounts of Bromelain and Papain are not required for daily health, they are extremely beneficial to ensure optimum digestion of proteins and absorption of nutrients. (oxfordvitality.co.uk)
  • Bromelain ist ein Enzym aus Ananas und Papain aus Papaya tropischen Kulturen. (alfafit.eu)
  • Papain is a natural cysteine proteolytic enzyme present in mountain papaya (Vasconcellea cundinamarcensis) and papaya (Carica papaya). (niir.org)
  • Increasing health awareness among consumers have a positive impact on natural proteolytic enzyme such as papain. (niir.org)
  • Papain is an enzyme coming from the papaya fruit ( Carica papaya ) that is used in the breakdown of proteins into amino acids during digestion (also known as a proteolytic enzyme). (oxfordvitality.co.uk)
  • Papain is a proteolytic enzyme that is made from the latex of the fruit of the papaya plant. (paperjaper.com)
  • The facility was a meat portioning plant which used the proteolytic enzyme meat tenderizer papain (9001734) as a component of spice mixtures sprayed on some steaks prior to packaging. (cdc.gov)
  • The papain precursor protein contains 345 amino acid residues, and consists of a signal sequence (1-18), a propeptide (19-133) and the mature peptide (134-345). (wikipedia.org)
  • Papain has wide specificity and it will degrade most protein substrates more extensively than the pancreatic proteases. (worthington-biochem.com)
  • The Papain produced in the fruit has been used for decades to aid in total digestion and significantly increase the nutrient absorption of protein based foods. (oxfordvitality.co.uk)
  • Papain is a protein that is found in the pineapple skin and stem. (paperjaper.com)
  • Papain is a protein-digesting enzyme derived from the fruit of the papaya, Carica papaya. (paperjaper.com)
  • Papain can further hydrolyze proteins in beer to produce more peptides or amino acids, making the wine more clarified and improving the taste of beer, effectively improving the quality of beer. (enzymes.bio)
  • Papain can be used to hydrolyze animal and plant proteins such as meat, beans, mushrooms, etc. and then used to produce chicken essence, oil, soy sauce, mushroom essence and other condiments. (enzymes.bio)
  • Papain is used in pharmaceutical and health care industry, mainly used to hydrolyze some specific animal and plant proteins into peptides or amino acids, such as the production of collagen peptide, soybean peptide, amino acid oral solution, etc. (enzymes.bio)
  • Papain breaks down proteins, carbohydrates, and fats. (medlineplus.gov)
  • The benefits of papain have long been recognized, and papain-rich products have been utilized to improve texture and quality. (marketresearchfuture.com)
  • With some tissues papain has proved less damaging and more effective than other proteases. (worthington-biochem.com)
  • Papain-like proteases that occur in species of CORONAVIRIDAE. (bvsalud.org)
  • Ingestion of papain from the papaya fruit is safe and healthy because the enzyme is destroyed by the acid in the stomach. (paperjaper.com)
  • Its ripe fruit is considered safe, but unripe papaya fruit contains papain and can damage the esophagus. (medlineplus.gov)
  • Unripe papaya fruit contains papaya latex, which contains an enzyme called papain. (medlineplus.gov)
  • There is some evidence that unprocessed papain, one of the chemicals found in unripe papaya fruit, might poison the fetus or cause birth defects. (medlineplus.gov)
  • If you've had the opportunity to look through our website, you should already know that papain comes from the water-soluble portion of the latex of Carica Papaya . (papain.com)
  • In immunology, papain is known to cleave the Fc (crystallisable) portion of immunoglobulins (antibodies) from the Fab (antigen-binding) portion. (wikipedia.org)
  • The Beta-Carotene/Papain Renewal Serum offers a mild exfoliation for sensitive skin. (dewdropesthetics.com)
  • Meat tenderisers in powder form with papain as an active component are widely sold and the culinary use of papaya peel has featured in research papers. (wikipedia.org)
  • Papain is an active component in powder form for meat tenderizers and has a huge demand in the global market. (niir.org)
  • The Papain market industry is projected to grow from USD 0.26 Billion in 2023 to USD 0.41 Billion by 2032, exhibiting a compound annual growth rate (CAGR) of 5.90% during the forecast period (2023 - 2032). (marketresearchfuture.com)
  • Furthermore, papain has numerous applications in the textile, personal care, and cosmetics industries, likely generating significant demand for papain during the papain market forecast period. (marketresearchfuture.com)
  • The North America papain market accounts for relatively high revenue share, followed by Western Europe papain market over the forecast period, attributed to relatively strong demand for papain and broad availability of raw material in the regions. (niir.org)
  • Among these, the pharmaceutical segment is expected to contribute to the significant revenue share with a relatively high growth rate over the forecast period in global papain market. (niir.org)
  • Taking large amounts of papain might damage the esophagus. (medlineplus.gov)
  • the skin of the papaya is placed directly on the wound due to it sourcing the highest concentration of Papain in the fruit. (oxfordvitality.co.uk)
  • Papain is extremely hard to purchase at the moment so we have imported it from overseas & broken it down into smaller bottles of 20 capsules. (hoptoitbunnies.com)
  • The mechanism by which papain breaks peptide bonds involves the use of a catalytic dyad with a deprotonated cysteine. (wikipedia.org)
  • The catalytic activity of papain in the synthesis of Z-Gly-Phe- NH2 in tert-butanol has been studied in the presence of solid- state acid-base buffers (acids and their sodium salts). (strath.ac.uk)
  • Hence, at least these buffers do not seem to be able to affect the protonation state and catalytic activity of papain. (strath.ac.uk)
  • Papain contains antioxidants and important nutrients such as vitamins A and C. As an antioxidant, papain contains chemicals that may protect the body from cellular damage caused by free radicals. (marketresearchfuture.com)
  • Increasing consumer needs for soft textured meat products for use is anticipated to escalate the market demand for papain on a global level. (niir.org)
  • When added to skin care products, papain can easily form complexes with copper ions in melanin to reduce the formation of pigmentation. (enzymes.bio)
  • But papain is changed in the stomach, so it's not clear if it's effective as medicine when taken by mouth. (medlineplus.gov)
  • Axcel Papain Tablet is used by a combination of physical meansor other chemotherapeutic to treat edema and inflammations. (royalepharma.com)
  • Papain breaks down tough meat fibres, and has been used since before European contact to tenderise meat eaten in its native South America. (wikipedia.org)
  • Papain is used worldwide in everything from food and beverages to medications, cosmetics, textiles, and animal feeds. (marketresearchfuture.com)
  • In the food industry, papain is used as an active ingredient in many commercial meat tenderizers. (wikipedia.org)
  • Due to farmers' increasing awareness of animal nutrition, the worldwide papain market is projected to see significant demand from the animal feed sector. (marketresearchfuture.com)
  • The papain industry has grown significantly due to increased consumer interest in health supplements. (marketresearchfuture.com)
  • Papain is a well-known enzyme with numerous applications in the animal feed industry, where it contributes to greater digestibility and nutrient-rich feed. (marketresearchfuture.com)
  • Global papain market is segmented by end-use industry and by region. (niir.org)
  • Papain in powdered or liquids forms are extensively used in the meat industry. (niir.org)
  • Papain is the main ingredient of Papacarie, a gel used for chemomechanical dental caries removal. (wikipedia.org)
  • Huettner and Baughman (1986) describe a method using papain to obtain high yields of viable, morphologically intact cortical neurons from postnatal rats. (worthington-biochem.com)
  • What foods are high in papain? (paperjaper.com)
  • Overall we have found that Papain is by far the most effective at moving the fur. (hoptoitbunnies.com)
  • As a result, prominent players are attempting to innovate to expand their papain product lines. (marketresearchfuture.com)