Tyrosine kinase substrate annexin II (p36) — biochemical characterization and conservation among species
نویسندگان
چکیده
منابع مشابه
Tyrosine kinase substrate annexin II (p36)--biochemical characterization and conservation among species.
secreted then degraded by endogenous proteases, because placental annexin 4 was not degraded when added to prostate fluid and incubated at 37°C. The collective concentrations of annexin 1 , des-( 1 -29)-annexin 1, and annexin 5 in prostate fluid and seminal plasma were 1.3% and 0.2% of the total protein, respectively. This is consistent with their secretion by the prostate and subsequent diluti...
متن کاملCloning and biochemical characterization of a plant protein kinase that phosphorylates serine, threonine, and tyrosine.
Phosphorylation of proteins on serine, threonine, or tyrosine residues represents an important biochemical mechanism to regulate the activity of enzymes and is used in many cellular processes. In animals, protein serine/threonine and protein tyrosine kinases are known to perform essential roles in many pathways that transmit external stimuli from the cell surface to the cell inferior and the nu...
متن کاملThe tight association of the tyrosine kinase substrate annexin II with the submembranous cytoskeleton depends on intact p11- and Ca(2+)-binding sites.
Annexin II, a member of the annexin family of Ca(2+)- and lipid-binding proteins, is a major substrate of the pp60src kinase. It is unique within the annexin protein family, since it can form a tight heterotetrameric complex with the cellular protein ligand p11, a member of the S100 protein family. Within the cell, the annexin II2p11(2) complex is localized at the cytoplasmic surface of the pla...
متن کاملBiochemical characterization of tyrosine kinase and phosphotyrosine phosphatase activities of HL-60 leukemia cells.
The cellular phosphotyrosine content of the HL-60 promyelocytic leukemia markedly decreased during the induced granulocytic and monocytic maturation of these cells. This occurs in the face of major increases in tyrosine kinase and protein phosphotyrosine phosphatase activities (D. A. Frank and A. C. Sartorelli, Biochem. Biophys. Res. Commun., 140: 440-447, 1986). In the present work, these two ...
متن کاملRat adrenocortical carcinoma 494 autophosphorylating protein kinase, autophosphorylating protein kinase 500. Purification, biochemical and immunological characterization, and substrate specificity.
A novel autophosphorylating protein kinase, autophosphorylating protein kinase 500, independent of cyclic AMP, cyclic GMP, calcium, and calmodulin was purified from rat adrenocortical carcinoma 494 by ammonium sulfate fractionation followed by the chromatographic steps of DEAE-cellulose, gel filtration, cyclic AMP-epoxy Sepharose, and phosphocellulose. Sometimes two additional chromatographic p...
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: Biochemical Society Transactions
سال: 1990
ISSN: 0300-5127,1470-8752
DOI: 10.1042/bst0181106