Bovine α2-antiplasmin N-Terminal and reactive site sequence
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چکیده
منابع مشابه
The N-terminal amino-acid sequence of bovine proparathyroid hormone.
Proparathyroid hormone (calcemic fraction-A) is a biosynthetic precursor of parathyroid hormone in bovine glands. Limited amounts of the isolated prohormone have been obtained for the purpose of initial structural studies. The results of automated sequence analysis on two separate preparations indicate that the N-terminal region of the prohormone consists of the sequence Lys-Ser-Val-Lys-Lys-Arg...
متن کاملNatural heterogeneity of α2-antiplasmin: functional and clinical consequences.
Human α2-antiplasmin (α2AP, also called α2-plasmin inhibitor) is the main physiological inhibitor of the fibrinolytic enzyme plasmin. α2AP inhibits plasmin on the fibrin clot or in the circulation by forming plasmin-antiplasmin complexes. Severely reduced α2AP levels in hereditary α2AP deficiency may lead to bleeding symptoms, whereas increased α2AP levels have been associated with increased th...
متن کاملAddition of a sequence from α2-antiplasmin transforms human serum albumin into a blood clot component that speeds clot lysis
BACKGROUND The plasma protein alpha2-antiplasmin (alpha2AP) is cross-linked to fibrin in blood clots by the transglutaminase factor XIIIa, and in that location retards clot lysis. Competition for this effect could be clinically useful in patients with thrombosis. We hypothesized that fusion of N-terminal portions of alpha2-antiplasmin to human serum albumin (HSA) and production of the chimeric ...
متن کامل[N-terminal sequence of a porphobilinogen synthase].
The N-terminal sequence of porphobilinogen-synthase (EC 4.2.1.24) from bovine liver up to position 44 is given. After tryptic hydrolysis two N-terminal peptides with identical amino acid composition were isolated in the ratio 1:1. One peptide was blocked whereas the other one started with methionine and showed the same primary structure which had been estimated by automatic degradation of the e...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1992
ISSN: 0014-5793
DOI: 10.1016/0014-5793(92)81419-m