Sequence comparison of pepsin-resistant segments of basement-membrane collagen alpha 1(IV) chains from bovine lens capsule and mouse tumour.
Sequence comparison of pepsin-resistant segments of basement-membrane collagen alpha 1(IV) chains from bovine lens capsule and mouse tumour.
复制标题
来自牛晶状体囊和小鼠肿瘤的基底膜胶原蛋白 α 1 (IV) 链的胃蛋白酶抗性片段的序列比较。
DOI：
10.1042/bj2200227
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发表时间：
1984
期刊：
影响因子：
--
通讯作者：
Kang,AH
中科院分区：
文献类型：
--
作者：
Schuppan,D;Glanville,RW;Timpl,R;Dixit,SN;Kang,AH
用溴化氰和胰蛋白酶切割牛晶状体囊胶原α 1（IV）链的C-末端消化片段P1（约518个氨基酸残基）。将肽纯化并表征，通过与小鼠胶原α 1（IV）链的相应部分比较，允许它们在P1片段内排序[Schuppan，Glanville和Timpl（1982）Eur. 123，505-512]。Edman降解法测定了P1片段67%的序列。与相应的小鼠胶原蛋白片段P1的序列的比较显示，对于三联体结构Gly-Xaa-Yaa的位置Xaa和Yaa，具有76%的同一性。发现两个非三联体中断和3-羟脯氨酸残基的位置的不变性，指出这些结构的功能的重要性。
The C-terminal peptic fragment P1 (about 518 amino acid residues) of bovine lens-capsule collagen alpha 1(IV) chain was cleaved with CNBr and trypsin. The peptides were purified and characterized, allowing their ordering within the P1 fragment by comparison with a corresponding section of mouse collagen alpha 1(IV) chain [Schuppan, Glanville & Timpl (1982) Eur. J. Biochem. 123, 505-512]. About 67% of the sequence of bovine collagen fragment P1 was determined by Edman degradation. Comparison with the sequence of the corresponding mouse collagen fragment P1 showed 76% identity for positions Xaa and Yaa of the triplet structures Gly-Xaa-Yaa. Invariance was found for the positions of two non-triplet interruptions and of 3-hydroxyproline residues, pointing to the functional importance of these structures.