Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.21.4 (trypsin)
 42,187 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Effects of treatments with proteolytic enzymes and protein-modifying reagents on flocculation of brewer's yeast IFO 2018 were investigated. The floc-forming ability of the yeast cells was irreversibly eliminated by treatment with papain, trypsin, chymotrypsin or pepsin, indicating that certain proteins on the cell surface participate in the yeast flocculation. Chemical modification with reagents, known to act on disulfide bridges, carboxyl and/or phosphate groups, phenolic groups, amino groups, and imidazole groups, also destroyed the ability to flocculate, although in some cases a high concentration (8 M) of urea was necessary in addition to protein-modifying reagents. Thus, it is suggested strongly that these functional groups of amino acid residues of the proteins are essential for the floc-forming ability of brewer's yeast cells.
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PMID:Effect of chemical modification of cell surface components of a brewer's yeast on the floc-forming ability. 33 19

Bovine serum IgG1, colostral IgG1 and serum IgG2 with anti-ferritin activity were digested with pepsin or trypsin. Their fragments were characterized by immunoelectrophoresis, gel electrophoresis and gel filtration; their ferritin-binding ability was determined. The kinetics of proteolysis were established by measuring the appearance of free amino groups. No differences were observed between serum and colostrum IgG1. IgG1 was more susceptible to pepsin, and IgG2 to trypsin. This became evident from both the amount of intact IgG determined by gel electrophoresis, immunoelectrophoresis or gel filtration, and from the kinetics of the appearance of amino groups. A model is presented to explain the size, mobilities and properties of the obtained fragments.
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PMID:Proteolysis of bovine immunoglobulins. 33 10

Using an in vitro procedure, with both plant (gluten and edestin) and animal proteins (egg white and casein) as ratio of protein substrate to enzymes (pepsin, trypsin, erepsin) was increased in progressive stages, there was a change in the amino acids released; the proportions of some amino acids progressively increased, others progressively decreased while still others remained constant. The pattern of amino acids released was distinct for each protein and as substrate increased relative to enzymes, certain amino acids essential for the human increased with some proteins and decreased with others which suggests nutritional implications. The variations in amino acids released with changes in ratio of substrate to enzymes was not a random effect but an apparent orderly process. The phenomenon is termed "variable ratio effect".
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PMID:Effect of ratio of enzymes to substrate on amino acid patterns released from proteins in vitro. 34 48

The light chain fraction was separated from rabbit skeletal muscle myosin and four kinds of light chains, L-1, L-2, L-3 and L-4 in the fraction were further isolated by column chromatography using DEAE-cellulose DE-52. After amino-ethylation, the L-2 light chain was digested with trypsin. It was also digested with chymotrypsin and pepsin, respectively, after carboxymethylation. Each of the tryptic, chymotryptic and peptic peptides thus obtained was separated and purified and their amino acid compositions were analyzed.
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PMID:The amino acid compositions of the tryptic, chymotryptic and peptic peptides from the L-2 light chain of rabbit skeletal muscle myosin. 34 67

The enzymes pepsin, alpha-chymotrypsin, trypsin, RNase and DNase were applied to preparations of human metaphase chromosomes before staining to study whether dissociable materials related to the formation of G-, Q- and C-bands would be seen. Treatment with active pepsin but not the other enzymes revealed material with ribonucleo-protein properties which dissociated from the chromosomes and formed a halo.--Lateral extensions from the chromatids stretched to the rim of the halo and appeared at positions corresponding to G-bands. A G-band may be defined as a ring of stable chromatid-matrix binding at positions where the chromatids coil to form lateral extensions.
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PMID:A pepsin-revealed material possibly related to chromosomal banding. 35 79

The aim of the present study was to describe the physicochemical characteristics of streptococcal T antigen. T protein isolated from Streptococcus pyogenes type 12 (R53/1077, Colindale) and purified by ion-exchange column chromatography resulted in a preparation that was homogeneous when tested electrophoretically (in two systems, in presence and in absence of sodium dodecyl sulfate) and by gel filtration on Sephadex G-100. The purified T antigen was resistant to enzymatic degradation by trypsin and pepsin. It formed a single precipitin line with standard T-12 antiserum and was not contaminated with group A carbohydrate and M protein. The molecular weight of protein T, determined by means of polyacrylamide gel electrophoresis and calculated from its amino acid composition, was about 39,000. The molecular weight of this protein, determined by means of high-speed sedimentation equilibrium, ranged between 80,000 and 120,000. Glutamic and asparatic acids, lysine, alanine, and leucine were the predominant amino acids.
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PMID:Characterization of group A streptococcal T-12 protein purified by ion-exchange column chromatography. 36 81

The nature of the intramitochondrial bodies in bovine adrenocortical cells was investigated both light and electron microscopically, by applying enzymatic digestion on paraffin and epon sections. The result that these bodies were extracted completely either by pepsin or by trypsin strengthened the validity of the previous conclusion that their nature is proteinaceous.
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PMID:Light and electron microscopic studies of intramitochondrial bodies in bovine adrenocortical cells by proteolytic digestion. 36 52

The effect of exposure to a sublethal concentration (0.30 mg/l) of mercuric chloride on the activities of alkaline phosphatase, acid phosphatase, amylase, trypsin, and pepsin has been examined at intervals of 7, 15, and 30 d in the digestive system of a teleost fish, Channa punctatus. Inhibition of the activities of all these enzymes was noted after the first week of treatment. Treatment of the fish for 15 d resulted in marked increases in the activities of all the enzymes. A slight fall in enzyme activity was recorded after 30 d, but the overall activity was higher than in control fish.
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PMID:Chronic mercuric chloride intoxication in digestive system of Channa punctatus. 36 60

Highly purified, papain-solubilized HLA-A, -B, and -C antigens comprising a mixture of a great number of allelic forms from at least three loci have been fragmented by limited proteolysis, acid cleavage, and cyanogen bromide treatment. Limited proteolysis of 125I-labeled HLA-A, -B, and -C antigens with trypsin, chymotrypsin, thermolysin, and pepsin resulted in the production of two large fragments. One fragment was associated with beta 2-microglobulin and contained all of the carbohydrate. The other fragment, which had a molecular weight of about 13,000, is most probably derived from the COOH-terminal part of the heavy chain. Acid cleavage of the HLA antigen heavy chain gave rise to two main fragments with molecular weights of 22,000 and 11,000. Both fragments contained disulfide bonds. Two minor components, representing further cleavage products of the 22,000-dalton fragment, were also observed. Cleavage of the HLA antigen heavy chain at methionyl residues gave rise to one carbohydrate-containing, cysteine-free 14,000-dalton fragment and one 20,000-dalton fragment that contained all cysteines but no carbohydrate. NH2-terminal amino acid sequence analyses demonstrated that the 22,000-dalton acid cleavage fragment and the 14,000-dalton cyanogen bromide fragment were derived from the NH2-terminal part of the HLA antigen heavy chain.
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PMID:Fragmentation of the human transplantation antigen heavy chain by limited proteolysis, acid cleavage, and cyanogen bromide treatment. 37 76

Gliadin, subsequently treated with pepsin, trypsin and pancreatic extract was further digested by small-intestinal mucosal homogenates from 10 control or 8 coeliac children. The amino acids liberated in the incubation mixture were measured and corrected for mucosal damage. In accordance with the data from the literature on adults, the total amount of amino acids released from gliadin peptides by the intestinal mucosa from children with active coeliac disease is significantly lower than that by the mucosa from control subjects. Qualitatively, however, no significant differences for the individual amino acids are observed with the exception of glutamine and proline, so that damaged coeliac mucosa liberates relatively more glutamine but less proline.
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PMID:Digestion of gliadin peptides by intestinal mucosa from control or coeliac children. 37 39


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