Identification and comparison of protein I in chick and rat forebrain.
Protein I has been identified and compared in membranes prepared from chick and rat forebrain. Based upon five criteria known to characterize protein I, namely, (1) its ability to serve as a substrate for both the cyclic AMP-dependent protein kinase and (2) the Ca2+- dependent, calmodulin-requiring protein kinase, (3) its ability to be extracted from membranes at low pH, (4) its characteristic pattern of digestion by collagenase, and (5) its existence as a basic protein, we have determined that although protein I of rat brain consists of the usual doublet polypeptides Ia and Ib, only a single chick forebrain polypeptide is detectable which possesses protein I-like properties.
D000818:Animals; D001923:Brain Chemistry; D002645:Chickens; D004591:Electrophoresis, Polyacrylamide Gel; D003012:Microbial Collagenase; D008970:Molecular Weight; D009419:Nerve Tissue Proteins / Q000032:analysis*; D010750:Phosphoproteins / Q000032:analysis*; D051381:Rats; D013045:Species Specificity; D016704:Synapsins; D013570:Synaptic Membranes / Q000032:analysis; D013574:Synaptosomes / Q000032:analysis*
D009419:Nerve Tissue Proteins; D010750:Phosphoproteins; D016704:Synapsins; D003012:Microbial Collagenase