Human prothrombin activation

Prothrombin domains: circular dichroic evidence for a lack of cooperativity

“…Proteins. Prothrombin was purified from titrated bovine plasma and from human Cohn fraction 3 (a gift of Dr. Charles Heldebrant, Abbott Laboratories) or from Red Cross factor IX concentrate (gift of Dr. Yu-Lee Hao, the American National Red Cross) as previously described (Downing et al, 1975;. Prothrombin fragment 1 and prethrombin 1 were prepared by proteolytic cleavage of prothrombin by thrombin and were separated as described elsewhere (Downing et al, 1975;Heldebrant et al, 1973).…”

“…Prothrombin was purified from titrated bovine plasma and from human Cohn fraction 3 (a gift of Dr. Charles Heldebrant, Abbott Laboratories) or from Red Cross factor IX concentrate (gift of Dr. Yu-Lee Hao, the American National Red Cross) as previously described (Downing et al, 1975;. Prothrombin fragment 1 and prethrombin 1 were prepared by proteolytic cleavage of prothrombin by thrombin and were separated as described elsewhere (Downing et al, 1975;Heldebrant et al, 1973). Prothrombin fragment 2, bovine prethrombin 2, and human prethrombin 2des(1_l3) were prepared by proteolytic cleavage of prethrombin 1 by factor Xa and were separated as previously described (Downing et al, 1975;Heldebrant et al, 1973).…”

“…The most readily isolated activation components of bovine and human prothrombin are1 (Mann, 1976) prothrombin 0006-2960/79/0418-1957S01.00/0 © 1979 American Chemical Society fragment 1 and prethrombin 1, produced by the thrombin catalyzed cleavage of prothrombin, and prothrombin fragment 2 and prethrombin 2, produced by a factor Xa catalyzed cleavage of prethrombin 1. The human protein differs from the bovine in that human prothrombin contains an additional thrombin-sensitive site (Downing et al, 1975). This additional site results in the liberation of an amino-terminal peptide of 13 residues from the A chain of human thrombin (and/or prethrombin 2).…”

Structural studies on rabbit transferrin: isolation and characterization of the glycopeptides

“…(B) Electrophoresis of 10 pg of reduced rabbit transferrin under a variety of denaturing conditions; (1) sodium dodecyl sulfate gel electrophoresis, 5% acrylamide; (2) acid-urea system, 10% acrylamide; (3) sodium dodecyl sulfate-urea gel electrophoresis, 12.5% acrylamide. Munkres (1971) as described by Downing et al (1975). Gels were stained for protein using Coomassie brilliant blue, and for carbohydrate by the use of the periodate-Schiff stain (Segrest & Jackson, 1972).…”

Διαταραχες Της Πηξεως Στην Οξεια Ιογενη Ηπατιτιδα Των Παιδιων

“…139 "Ολοι είναι γλυκοπρωτεΐνες μέ μιά αλυσο καί μοριακό βάρος 72-54.00. 44 ' Ηπατοκυτταρική βλάβη καί χορήγηση κουμαρινικών παραγώγων έχουν σάν αποτέλεσμα τή μειωμένη σύνθεση καί των 4 αυτών παραγόν των, 40 ενώ κατά τή διάρκεια εγκυμοσύνης τά επίπεδα τους αυξάνονται. "Ολοι προσροφώνται άπό τό φωσφορικό ασβέστιο, τό υδροξείδιο τοϋ άργιλίου ή τό θειικό βάριο, όλοι έχουν τήν ίδια σταθερά θερμοκρασίας καί είναι σταθεροί στους -20°C γιά μεγάλο διάστημα, σέ αντίθεση μέ τους πα ράγοντες V καί VIII, πού είναι ασταθείς παράγοντες.…”