Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.21.7 (plasmin)
 9,023 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Plasminogen was found to be present in bovine milk by crossreactivity between rabbit antiserum to plasminogen and casein prepared from milk by acid precipitation. This result was further supported by recovery of intact 125I-labeled plasminogen from rabbit milk after its intravenous injection. Freshly isolated whole bovine casein was observed to undergo slow autoproteolysis at 37 degrees C. Polyacrylamide gel electrophoresis revealed gradual disappearance of major caseins accompanied by appearance and increase in intensity of numerous electrophoretic bands. This autoproteolysis was inhibited by low concentrations of epsilon-aminocaproic acid (0.1 mM) and diisopropyl fluorophosphate (1 mM); catalytic amounts of urokinase accelerated the process. Autoproteolysis of isolated bovine beta-casein was shown by both urea and sodium dodecyl sulfate gel electrophoresis to result in formation of gamma 1- and gamma 2-caseins. Similar electrophoretic bands were formed when beta-casein was degraded by plasmin prepared from bovine blood serum. These results support the hypothesis that bovine plasmin occurs in milk and is identical to alkaline milk protease.
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PMID:Plasmin-mediated proteolysis of casein in bovine milk. 15 65

A total of 367 milk samples were collected from 43 individual Holstein cows during 1 yr. Samples were analyzed for plasmin activity, total casein, alpha s-casein (alpha s1-casein + alpha s2-casein), beta-casein, kappa-casein, and SCC. Least squares analyses showed that SCC in milk were positively related (r = .62) to plasmin activity. An increase of SCC from 100,000 to 1,300,000/ml was associated with a 2.3-fold increase in plasmin activity (100 vs. 230 x 10(-6) units/ml). Increased plasmin activity was associated with advancing stage of lactation and older cows after appropriate adjustments were made for the effects of milk yield and SCC. Milk samples obtained in fall and winter were higher, but not significantly, in plasmin activity. Plasmin activity was also associated with major casein components and milk pH. Correlations coefficients between plasmin and alpha s-casein, beta-casein, and pH were -.14, -.27, and .19.
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PMID:Environmental factors affecting plasmin activity in milk. 252 74

A new peptide of 20,000 daltons was found in human milk as a constituent of the casein micelle. Enzymic digestion with plasmin or trypsin revealed that the peptide was identical with a degradation product of human beta-casein. The amino acid composition of the degradation product and the previously reported sequence in the N-terminal region of human beta-casein suggested that the peptide was a fragment of beta-casein lacking the C-terminal region. The thermal sensitivity of this peptide was higher than that of beta-casein, but the peptide lost the property of calcium-dependent precipitation, which intact beta-casein possesses.
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PMID:A 20,000-dalton casein fragment in human milk. 293 32

A method is described for preparing immunologically homogeneous human milk beta-casein, against which monospecific rabbit antiserum was prepared. The antiserum was used to quantify beta-casein, the major human casein, by rocket immunoelectrophoresis in individual milk samples. However, it was found that in most samples beta-casein occurred together with degradation products originating from its proteolysis by plasmin. Immunological quantification of human beta-casein, treated with plasmin for various time periods, showed that rocket height was not affected by proteolysis up to degradation states clearly more advanced than those observed in all samples of fresh human milk tested. Assays of 150 individual milk samples from 80 women, covering a lactation period of up to 730 d, gave an average concentration of beta-casein (native + degraded) of 4.67 +/- 0.89 standard deviation (g/l); extremes at 2.1 and 7.3 g/l did not vary significantly during the period under study. Comparison of this average value with an accepted casein content of 4.4 g/l (Macy & Kelly, 1961) showed that the casein content of human milk is underestimated when obtained by N determinations on milk and on its supernatants at pH 4.6 (whey). Caseins other than beta-casein occurred only in minute amounts, if at all.
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PMID:Quantification of beta-casein in human milk. 315 66

Three peptides have been formed by proteolytic digestion of individual casein proteins and their secondary structures characterised by far-UV circular dichroism (CD). Peptide alpha s1(1-23), residues 1-23 of alpha s1-casein, was generated by treatment of the parent protein with chymosin. Peptides beta(1-28) and beta(1-52), residues 1-28 and 1-52 of beta-casein, were plasmin- and chymotrypsin-generated fragments, respectively. Analysis of the CD spectra revealed that in aqueous solution all three peptides have secondary structures composed exclusively of beta-sheet and random coil. A limited amount of alpha-helix was formed in two of the three peptides upon treatment with high concentrations (greater than 40% (v/v] of 2,2,2-trifluoroethanol. Partial dephosphorylation (60%) of beta(1-28) and beta(1-52) by treatment with alkaline phosphatase resulted in homogeneous preparations, as judged by polyacrylamide gel electrophoresis, which exhibited increased hydrophobicity. This reduction in the level of phosphorylation of serine residues 15, 17, 18 and 19 led to increased propensity for helix formation in the peptides in the presence of 2,2,2-trifluoroethanol, but no alpha-helical structures were detected in the dephosphorylated peptides in the absence of 2,2,2-trifluoroethanol.
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PMID:The secondary structure of peptides derived from caseins: a circular dichroism study. 316 68

Three groups of casein components were isolated from horse milk. Group I is almost insoluble at acid and neutral pH, and is rather heterogeneous on alkaline gels with or without sodium dodecyl sulphate. Group II shows strong similarity to beta-casein from other species, as concluded from its amino acid composition and its N- and C-terminal sequences. This group consists of five electrophoretically distinguishable forms, all containing ester phosphate groups but no carbohydrate. Group III is composed of C-terminal fragments of the beta-like (group II) fraction and probably arises from the action of a plasmin-like enzyme present in horse milk. It does not contain phosphate or carbohydrate. Homology of this group with bovine gamma-caseins is demonstrated. Both beta- and gamma-like caseins are more soluble at 4 degrees C than at room temperature.
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PMID:Isolation and characterization of beta- and gamma-caseins from horse milk. 621 24

Proteolytic activity in mastitic skim-milk was often 5-10 fold higher than in normal milk, its level being related to somatic cell count but not precisely correlated with it. In milks with the highest levels of activity plasmin accounted for about one third of the total proteinase. A further third was sedimented with the micellar fraction together with the plasmin, but unlike plasmin, was not inhibited by addition of soyabean trypsin inhibitor (SBTI). The final third remained in the serum phase. Polyacrylamide gel electrophoresis (PAGE) showed that alpha-sl- and beta-caseins were degraded at about the same overall rate. The plasmin produced the usual readily identified fragments from beta-casein, but incubation of mastitic milk also produced changes in patterns in the gamma-casein region differing from plasmin-induced changes, which were also apparent when the micellar fraction was incubated. As they were inhibited by SBTI, a second trypsin-like enzyme in addition to plasmin may also have been present. Other proteinase(s) not inhibited by SBTI was also associated with casein micelles and produced at least 3 characteristic protein fragments seen on PAGE. The serum phase proteinase(s) was likewise not inhibited by SBTI, and did not produce any well-defined electrophoretic bands, suggesting a rather non-specific breakdown of caseins. After separation of mastitic whole milk, a considerable proportion of the proteolytic activity was found in the cream phase. The proportion was enhanced by freezing and thawing, and the enzyme appeared to be identical to the SBTI-resistant micellar proteinase. Because of the considerable proteolysis likely to occur under the time and temperature conditions involved, our results may provide some explanation for the problems encountered in cheesemaking with mastitic milks (e.g. yield losses, poor curd strength and off-flavour development).
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PMID:Qualitative and quantitative determination of proteolysis in mastitic milks. 621 34

Plasmin cleaves isolated human beta-casein to form specific fragments in a manner similar to the generation of gamma 1-, gamma 2-, and gamma 3-caseins from the bovine homologue. Identification of a protein previously isolated from human milk as a specific plasmin cleaved portion of beta-casein indicates that endogenous plasmin is active in whole milk. These findings suggest that protease activity should be considered in casein quantitation or isolation of components from human milk.
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PMID:Plasmin cleaves human beta-casein. 624 Feb 66

Native proteolytic enzymes in good quality normal bovine milk readily hydrolysed the caseins during incubation or storage, producing the gamma-caseins, proteose-peptone components 5 (PP5) and 8-fast (PP8F) and a considerable number of other unidentified fragments, many of which were also subsequently found in the proteose-peptone fraction. The rate of casein hydrolysis was greater in pasteurized than in raw milk, with beta-casein being slightly more susceptible to attack than alpha S1-casein. Measurements of gamma-casein and proteose-peptone formation have been made and it was found that PP5 was an intermediate product that was subject to further proteolysis while PP8F was a stable end-product. With the exception of component 3 (PP3), virtually all constituents of the proteose-peptone fraction increased during storage and appeared to be products of the action of proteolytic enzymes. Further evidence was obtained from the effects of various inhibitors that the principal proteinase of normal milk is plasmin, but slight differences were apparent between the protein breakdown patterns induced by storage and by added plasmin, which was consistent with the presence of more than one proteinase. Incubations in the presence of soya bean trypsin inhibitor to prevent plasmin action clearly revealed that another enzyme(s) was also involved.
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PMID:Proteinases in normal bovine milk and their action on caseins. 634 22

Milk obtained from cows which were either infected by clinical mastitis or had been subjected to intramammary infusion of Escherichia coli endotoxin possessed high counts of somatic cells and very high levels of proteinase activity which hydrolysed the caseins almost completely in a few hours at 37 degrees C. The rate of hydrolysis of beta-casein was slightly greater than that of alpha S1-casein, but in both cases hydrolysis was enhanced by 6 cycles of freezing and thawing to disrupt somatic cell membranes. A study of the relationship between proteinase activity and cell count suggested that only some of the proteinase activity originated in the somatic cells and also that the identity of the cells making up the total cellular population was important. Maximum proteolysis occurred at 50-60 degrees C, but the temperature-activity curve was a broad peak. Likewise the pH versus activity plot was very broad and was almost flat over the pH range 6-9. Experiments with a number of inhibitors of proteinases failed to give a clear cut pattern of inhibition. All evidence obtained was consistent with the view that several different enzymes with different pH and temperature optima and different specificities contributed to the overall hydrolysis of caseins in these milks. From electrophoretic band patterns one of these enzymes was clearly plasmin, but in high cell count milks other proteinases also became significant.
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PMID:Breakdown of caseins by proteinases in bovine milks with high somatic cell counts arising from mastitis or infusion with bacterial endotoxin. 634 23


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