Kenny A J, Booth A G, Macnair R D
Curr Probl Clin Biochem. 1977;8:46-58.
The membrane of kidney microvilli is richly endowed with peptidases. Present information is that there are at least eight examples located in this membrane. Three of the group are known to be among the major proteins that can be identified by dodecyl sulphate electrophoresis of the purified microvillus fraction. These three peptidases, aminopeptidase M, serine peptidase (dipeptidyl peptidase IV) and neutral endopeptidase can be labelled by lactoperoxidase iodination from either the luminal or the inner surfaces of the membrane, a result consistent with the view that the polypeptide chains span the microvillus membrane. The serine peptidase has been purified by two methods, permitting a comparison of the detergent-released and proteinase-released forms. The two forms differ in the presence and absence of the hydrophobic anchor that secures the enzyme to the membrane. Preliminary studies support the view that this hydrophobic domain is relatively small and that it includes the N-terminal region of the polypeptide chain.
肾微绒毛膜富含肽酶。目前的信息表明，该膜中至少有八个例子。已知该组中的三种是可通过纯化的微绒毛部分的十二烷基硫酸盐电泳鉴定的主要蛋白质之一。这三种肽酶，氨肽酶M、丝氨酸肽酶（二肽基肽酶IV）和中性内肽酶可以通过乳过氧化物酶碘化从膜的腔面或内表面进行标记，这一结果与多肽链跨越微绒毛膜的观点一致。丝氨酸肽酶已通过两种方法纯化，从而可以比较去污剂释放形式和蛋白酶释放形式。这两种形式在是否存在将酶固定在膜上的疏水锚方面有所不同。初步研究支持这样的观点，即该疏水域相对较小，并且它包括多肽链的N端区域。
