Hostname: page-component-586b7cd67f-t7czq Total loading time: 0 Render date: 2024-12-04T19:37:28.075Z Has data issue: false hasContentIssue false

Plasmin activity and proteose-peptone content of individual milks

Published online by Cambridge University Press:  01 June 2009

Johan Schaar
Affiliation:
Department of Animal Breeding and Genetics, Swedish University of Agricultural Sciences, S-750 07 Uppsala, Sweden

Summary

The variation in plasmin activity and proteose-peptone (PP) content in milks from 81 cows of four breeds was statistically analysed. Plasmin activity increased with parity and stage of lactation and differed between breeds, but the breed effect was removed when adjustment was made for differences in milk casein content. The negative correlation found between plasmin activity and casein content seemed to be expressed only under assay conditions and was thus probably an artefact. The linear regressions of proteose-peptones in fresh (PP) and cold-stored milks (ΔPP) on plasmin activity were highly significant (P < 0·001). However, the variation in plasmin activity explained only 38 and 33%, respectively, of the variation in PP and ΔPP. At apparent zero plasmin activity, PP and ΔPP were significantly different from zero (P < 0·001) and the intercepts represented 77 and 46%, respectively, of the averages. PP and ΔPP were significantly higher in milks containing the BB genotype of ²-lactoglobulin than in milks with the AA genotype.

Type
Original Articles
Copyright
Copyright © Proprietors of Journal of Dairy Research 1985

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

Ahrné, L. & Björok, L. 1985 Lipolysis and the distribution of lipase activity in bovine milk in relation to stage of lactation and time of milking. Journal of Dairy Research 52 5564CrossRefGoogle ScholarPubMed
Aimutis, W. R. & Eigel, W. N. 1982 Identification of »-casein as plasmin-derived fragments of bovine ±s1-casein. Journal of Dairy Science 65 175181CrossRefGoogle Scholar
Andrews, A. T. 1979 The formation and structure of some proteose-peptone components. Journal of Dairy Research 46 215218CrossRefGoogle ScholarPubMed
Andrews, A. T. 1983 Breakdown of caseins by proteinases in bovine milks with high somatic cell counts arising from mastitis or infusion with bacterial endotoxin. Journal of Dairy Research 50 5766CrossRefGoogle ScholarPubMed
Andrews, A. T. & Auichanidis, E. 1983 Proteolysis of caseins and the proteose-peptone fraction of bovine milk. Journal of Dairy Research 50 275290CrossRefGoogle ScholarPubMed
Barry, J. G. & Donnelly, W. J. 1980 Casein compositional studies. I. The composition of casein from Friesian herd milks. Journal of Dairy Research 47 7181CrossRefGoogle Scholar
Barry, J. G. & Donnelly, W. J. 1981 Casein compositional studies. II. The effect of secretory disturbance on casein composition in freshly drawn and aged bovine milks. Journal of Dairy Research 48 437446CrossRefGoogle Scholar
Bienkowski, R. S. 1983 Intracellular degradation of newly synthesized secretory proteins. Biochemical Journal 214 110CrossRefGoogle ScholarPubMed
Collen, D. 1980 On the regulation and control of fibrinolysis. Thrombosis & Haemostasis 43 7789Google ScholarPubMed
Davies, D. T. & Law, A. J. R. 1977 The composition of whole casein from the milk of Ayrshire cows. Journal of Dairy Research 44 447454CrossRefGoogle Scholar
De Rham, O. & Andrews, A. T. 1982 Qualitative and quantitative determination of proteolysis in mastitic milks. Journal of Dairy Research 49 587596CrossRefGoogle ScholarPubMed
Donnelly, W. J. & Barry, J. G. 1983 Casein compositional studies. III. Changes in Irish milk for manufacturing and role of milk proteinase. Journal of Dairy Research 50 433441CrossRefGoogle Scholar
Eigel, W. N. 1977 Formation of »1-A2, »2-A2 and »3-A caseins by in vitro proteolysis of β-casein A2 with bovine plasmin. International Journal of Biochemistry 8 187192CrossRefGoogle Scholar
Fox, P. F. 1981 Proteinases in dairy technology. Netherlands Milk and Dairy Journal 35 233253Google Scholar
Hillier, R. M. & Cheeseman, G. C. 1979 Effect of proteose-peptone on the heat gelation of whey protein isolates. Journal of Dairy Research 46 113120CrossRefGoogle Scholar
Kaminogawa, S., Mizobuchi, H. & Yamauchi, K. 1972 Comparison of bovine milk protease with plasmin. Agricultural and Biological Chemistry 36 21632167CrossRefGoogle Scholar
Kanno, C. & Yamauchi, K. 1979 Relationship of soluble glycoprotein of milk fat globule membrane to component-3, -5 and -8 fractions of proteose-peptone. Agricultural and Biological Chemistry 43 21052113Google Scholar
Kester, J. J. & Brunner, J. R. 1982 Milk fat-globule membrane as possible origin of proteose-peptone glycoproteins. Journal of Dairy Science 65 22412252CrossRefGoogle Scholar
Korycka-Dahl, M., Ribadeau Dumas, B., Chene, N. & Martal, J. 1983 Plasmin activity in milk. Journal of Dairy Science 66 704711CrossRefGoogle Scholar
Kristensen, P., Larsson, L. -I., Nielsen, L. S., Grøndahl-Hansen, J., Andreasen, P. A. & Danø, K. 1984 Human endothelial cells contain one type of plasminogen activator. FEBS Letters 168 3337CrossRefGoogle ScholarPubMed
Larsson, L. -I., Skriver, L., Nielsen, L. S., Grøndahl-Hansen, J., Kristensen, P. & Danø, K. 1984 Distribution of urokinase-type plasminogen activator immunoreactivity in the mouse. Journal of Cell Biology 98 894903CrossRefGoogle ScholarPubMed
McLean, D. M., Graham, E. R. B., Ponzoni, R. W. & McKenzie, H. A. 1984 Effects of milk protein genetic variants on milk yield and composition. Journal of Dairy Research 51 531546CrossRefGoogle ScholarPubMed
Okamoto, U., Horie, N., Nagiamatsu, Y. & Yamamot, J. -I. 1981 Plasminogen-activator in human early milk: Its partial purification and characterization. Thrombosis & Haemostasis 45 121126Google ScholarPubMed
Ossowski, L., Biegel, D. & Reich, E. 1979 Mammary plasminogen activator: cor elation with involution, hormonal modulation and comparison between normal and neoplastic tissue. Cell 1 929940CrossRefGoogle Scholar
Razooki Hasan, H., White, D. A. & Mayer, R. J. 1982 Extensive destruction of newly synthesized casein in mammary explants in organ culture. Biochemical Journal 202 133138CrossRefGoogle ScholarPubMed
Richardson, B. C. 1983 Variation of the concentration of plasmin and plasminogen in bovine milk with lactation. New Zealand Journal of Dairy Science and Technology 18 247252Google Scholar
Richardson, B. C. & Pearce, K. N. 1981 The determination of plasmin in dairy products. New Zealand Journal of Dairy Science and Technology 16 209220Google Scholar
SAS Institute Inc. 1982 SAS User's Guide: Statistics. Gary, NC: SAS Institute Inc.Google Scholar
Schaar, J. 1984 Effects of κ-casein genetic variants and lactation number on the renneting properties of individual milks. Journal of Dairy Research 51 397406CrossRefGoogle Scholar
Sjaunja, L. -O. & Schaar, J. 1984 Determination of casein in milk by infrared spectrophotometry. Milchwissenschaft 39 288290Google Scholar
Snoeren, T. H. M. & Van Riel, J. A. M. 1979 Milk proteinase, its isolation and action on αs2- and β-casein. Milchwissenschaft 34 528531Google Scholar
Snoeren, T. H. M., Van Riel, J. A. M. & Both, P. 1980 [Some properties of a milk proteinase isolated from UHT-treated milk.] Zuivelzicht 72 4243Google Scholar