Isolation and characterization of two α chain size collagenous polypeptide chains c and d from glomerular basement membrane
Isolation and characterization of two α chain size collagenous polypeptide chains c and d from glomerular basement membrane
复制标题
肾小球基底膜中两条 α 链大小的胶原多肽链 c 和 d 的分离和表征
DOI:
10.1016/0014-5793(79)80536-0
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发表时间:
1979
期刊:
影响因子:
3.5
通讯作者:
S. Dixit
中科院分区:
文献类型:
--
作者:
S. Dixit
Basement membranes are extracellular structures composed of collagenous protein (s), one or more glycoproteins and~ yco~ minoglycans [l-3]. At the present time, the chemical structure of the collagenous component and its molecular organization remain controversial. The collagen component (s) of basement membrane constitutes a genetically distinct class of collagen differing from types I, II and III collagen by the presence of higher contents of 3-hydroxyproline, hydroxylysine, leucine, and carbohydrate and low contents of alanine. Kefalides [4-61 described an (II chain size basement membrane collagenous component (type IV), obtained from the pepsin digest of lens capsule, glomerulus, and descemet’s membrane. Timpl et al.[7] have estimated that molecular weight of type IV collagen is> 400 000. Other investigators [&lo] have published results indicating the heterogenous nature of the collagenous component of glomerular basement membrane. Q Chain size polypeptide chains A and B have been isolated from placenta, liver, skin, and the medial layer of vascular tissues [1 ll 31. Similar chains A and B have also been reported from placenta [14], bovine skeletal muscle [151, synovial membrane and* Nomenclature: The nomenclature of C and D chains presented in this paper corresponds to one used by Kresina, Rhodes and Miller (1978) Fed. Proc. FASEB 37 (6), 1528. The C and D chains have also been referred to as cul (IV) and & (IV) chains, respectively, by Dr Paul Bornstein