Back to Search Start Over

An angiogenic protein from bovine serum and milk--purification and primary structure of angiogenin-2.

Authors :
Strydom DJ
Bond MD
Vallee BL
Source :
European journal of biochemistry [Eur J Biochem] 1997 Jul 15; Vol. 247 (2), pp. 535-44.
Publication Year :
1997

Abstract

Bovine serum and milk contain a basic angiogenic protein that binds tightly to placental ribonuclease inhibitor. It was purified from both sources by ion-exchange and reversed-phase chromatographies. Its amino acid sequence revealed that it is a member of the ribonuclease superfamily. It contains 123 amino acids in a single polypeptide chain, is cross-linked by three disulfide bonds, is glycosylated at Asn33, and is 57% identical to bovine angiogenin. The amino-terminal and carboxyl-terminal residues are pyroglutamic acid and proline, respectively. The protein has ribonucleolytic activity that is similar to, but somewhat lower than, that of bovine angiogenin, i.e. very low relative to RNase. It is angiogenically potent on chicken chorioallantoic membrane, but less so than angiogenin. The sequence and activities demonstrate that this protein is a second, distinct, member of the angiogenin sub-family of pancreatic ribonucleases, and is referred to as angiogenin-2.

Details

Language :
English
ISSN :
0014-2956
Volume :
247
Issue :
2
Database :
MEDLINE
Journal :
European journal of biochemistry
Publication Type :
Academic Journal
Accession number :
9266695
Full Text :
https://doi.org/10.1111/j.1432-1033.1997.00535.x