AMINO-TERMINAL SEQUENCES OF 2 POLYPEPTIDES FROM HUMAN-SERUM WITH NONSUPPRESSIBLE INSULIN-LIKE AND CELL-GROWTH-PROMOTING ACTIVITIES - EVIDENCE FOR STRUCTURAL HOMOLOGY WITH INSULIN B CHAIN
AMINO-TERMINAL SEQUENCES OF 2 POLYPEPTIDES FROM HUMAN-SERUM WITH NONSUPPRESSIBLE INSULIN-LIKE AND CELL-GROWTH-PROMOTING ACTIVITIES - EVIDENCE FOR STRUCTURAL HOMOLOGY WITH INSULIN B CHAIN
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DOI：
10.1073/pnas.73.12.4379
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发表时间：
1976-01-01
影响因子：
11.1
通讯作者：
HUMBEL, RE
中科院分区：
文献类型：
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作者：
RINDERKNECHT, E;HUMBEL, RE
测定了从人血清中分离的2种具有非抑制性胰岛素样和细胞生长促进活性的多肽（NSILA I和II）的氨基末端序列。在前31个残基中，22个在NSILA I和II中是相同的。发现NSILA与胰岛素B链之间具有惊人的结构相似性：NSILA I中47%和57%的残基1-30分别与人和金枪鱼胰岛素B链中的残基相同。这种高度的序列同一性是胰岛素和NSILA同源性和共同进化起源的证据。基于这些结果和前面描述的NSILA的生物学特性，提出了NSILA的新名称：胰岛素样生长因子（IGF）。
The amino-terminal sequences of 2 polypeptides with nonsuppressible insulin-like and cell-growth-promoting activities (NSILA I and II), isolated from human serum, were determined. Of the first 31 residues, 22 are identical in NSILA I and II. A striking structural similarity was found between NSILA and insulin B chain: 47 and 57% of residues 1-30 in NSILA I are identical to those in insulin B chain from man and tuna fish, respectively. This high degree of sequence identity is presented as evidence for homology and for a common evolutionary origin of insulin and NSILA. Based on these results and on biological properties of NSILA described earlier, a new designation for NSILA is proposed: insulin-like growth factor (IGF).