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- W1987948710 endingPage "544" @default.
- W1987948710 startingPage "535" @default.
- W1987948710 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." @default.
- W1987948710 created "2016-06-24" @default.
- W1987948710 creator A5020132888 @default.
- W1987948710 creator A5044161672 @default.
- W1987948710 creator A5071054945 @default.
- W1987948710 date "1997-07-15" @default.
- W1987948710 modified "2023-09-27" @default.
- W1987948710 title "An Angiogenic Protein from Bovine Serum and Milk - Purification and Primary Structure of Angiogenin-2" @default.
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