Tb3+ binding to bovine prothrombin and bovine prothrombin fragment 1.
نویسندگان
چکیده
منابع مشابه
The effect of divalent metal ions on the electrophoretic mobility of bovine prothrombin and bovine prothrombin fragment 1.
Examination of metal ion-dependent effects on the electrophoretic mobility of bovine prothrombin and fragment 1 provides a useful and sensitive method for investigation of conformational processes in these proteins. Utilization of this method reveals a conformational change in bovine prothrombin and fragment 1 which occurs at low metal ion concentrations. Equilibrium dialysis studies indicate t...
متن کاملPhospholipid binding properties of bovine prothrombin peptide residues 1-45.
The present study investigates the unique contribution of the NH2-terminal 33 residues of prothrombin, the gamma-carboxyglutamic acid (Gla) domain, to the Ca(II) and phospholipid-binding properties of prothrombin. Two Gla domain peptides, 1-42 and 1-45, produced by chymotryptic cleavage of prothrombin fragment 1 (residues 1-156 of the amino terminus of bovine prothrombin) and isolated by anion-...
متن کاملThe Carbohydrate of Bovine Prothrombin
The inner carbohydrate was resistant to enzymatic attack and consisted of about one-third of the total mannose and one-half of the total iV-acetylglucosamine residues. It was shown that the carbohydrate chain was not attached to serine or threonine and that it is probably linked to asparagine. The cx and p anomeric forms of galactose were present in about a 1: 1 ratio. Glycopeptides containing ...
متن کاملSolution conformations of the gamma-carboxyglutamic acid domain of bovine prothrombin fragment 1, residues 1-65.
Molecular dynamics simulations have been performed (AMBER version 3.1) on solvated residues 1-65 of bovine prothrombin fragment 1 (BF1) by using the 2.8-A resolution crystallographic coordinates as the starting conformation for understanding calcium ion-induced conformational changes that precede experimentally observable phospholipid binding. Simulations were performed on the non-metal-bound c...
متن کاملCloning and analysis of a cDNA coding for bovine prothrombin.
Poly(A)-RNA enriched for prothrombin was isolated by specific immunoprecipitation of bovine liver polysomes. Prothrombin consisted of about 8% of the cell-free translation products of this RNA. A double-stranded cDNA was synthesized by using reverse transcriptase (RNA-dependent DNA nucleotidyltransferase) and made blunt-ended with nuclease S1. After tailing with dCTP and terminal transferase, t...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1985
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)85102-5