Sorensen R G, Babitch J A
J Neurochem. 1984 Mar;42(3):705-10. doi: 10.1111/j.1471-4159.1984.tb02740.x.
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.
已在从鸡和大鼠前脑制备的膜中鉴定并比较了蛋白质I。基于已知可表征蛋白质I的五个标准，即：（1）其作为环磷酸腺苷依赖性蛋白激酶和（2）钙依赖性、钙调蛋白依赖性蛋白激酶底物的能力，（3）其在低pH下从膜中提取的能力，（4）其被胶原酶消化的特征模式，以及（5）其作为碱性蛋白的存在，我们已确定，尽管大鼠脑的蛋白质I由通常的双峰多肽Ia和Ib组成，但仅可检测到一种具有蛋白质I样特性的鸡前脑多肽。
