JDS
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Journal of Dairy Science Vol. 80 No. 8 1490-1496
© 1997 by American Dairy Science Association ®
This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Precetti, A. S.
Right arrow Articles by Nielsen, S. S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Precetti, A. S.
Right arrow Articles by Nielsen, S. S.

Presence in Bovine Milk of Two Protease Inhibitors of the Plasmin System

A. S. Precetti 1, M. P. Oria 1, and S. S. Nielsen 1

1 Department of Food Science, Purdue University, West Lafayette, IN 47907

Proteolysis, caused by the serine proteinase plasmin (EC 3.4.21.7) that is present in milk, influences the quality of dairy products. Within the plasmin system, activators and inhibitors control plasmin activity. This study investigated the presence in bovine milk of two serine proteinase inhibitors of the plasmin system, alpha2-antiplasmin and plasminogen activator inhibitor-1, and an isolation procedure used for partial purification of them from milk. Two colorimetric assays were used to detect either plasmin inhibitor activity or plasminogen activator inhibitor activity. Two inhibitors were partially purified from milk using a combination of ammonium sulfate fractionation and concanavalin A affinity chromatography. Plasminogen activator inhibitor-1 and alpha2-antiplasmin antigens, which were associated with the inhibitory activities from bovine milk, were visualized by Western blot using commercial polyclonal antibodies raised against the corresponding human inhibitors. Both inhibitors were present in milk as several forms, possibly from the formation of complexes with other milk proteins. The predominant forms of the inhibitors in milk exhibited an approximate molecular mass of 60 kDa for alpha2-antiplasmin and 55 kDa for plasminogen activator inhibitor-1.

Key Words: serine proteinase inhibitor • bovine plasmin • alpha2-antiplasmin • plasminogen activator inhibitor-1

Submitted on June 14, 1996
Accepted on January 10, 1997




This article has been cited by other articles:


Home page
J DAIRY SCIHome page
B. Ismail, L. H. Choi, L. M. Were, and S. S. Nielsen
Activity and nature of plasminogen activators associated with the casein micelle.
J Dairy Sci, September 1, 2006; 89(9): 3285 - 3295.
[Abstract] [Full Text] [PDF]


Home page
J DAIRY SCIHome page
B. K. Nelson and D. M. Barbano
Yield and Aging of Cheddar Cheeses Manufactured from Milks with Different Milk Serum Protein Contents
J Dairy Sci, December 1, 2005; 88(12): 4183 - 4194.
[Abstract] [Full Text] [PDF]


Home page
J DAIRY SCIHome page
D. Borda, Indrawati, C. Smout, A. Van Loey, and M. Hendrickx
High Pressure Thermal Inactivation Kinetics of a Plasmin System
J Dairy Sci, August 1, 2004; 87(8): 2351 - 2358.
[Abstract] [Full Text] [PDF]


Home page
J DAIRY SCIHome page
A. Shamay, F. Shapiro, G. Leitner, and N. Silanikove
Infusions of Casein Hydrolyzates into the Mammary Gland Disrupt Tight Junction Integrity and Induce Involution in Cows
J Dairy Sci, April 1, 2003; 86(4): 1250 - 1258.
[Abstract] [Full Text] [PDF]


Home page
J DAIRY SCIHome page
M. R. Garcia-Risco, I. Recio, E. Molina, and R. Lopez-Fandino
Plasmin Activity in Pressurized Milk
J Dairy Sci, March 1, 2003; 86(3): 728 - 734.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1997 by the American Dairy Science Association ®.