PLASMINOGEN-ACTIVATOR INHIBITOR TYPE-1 - REACTIVE CENTER AND AMINO-TERMINAL HETEROGENEITY DETERMINED BY PROTEIN AND CDNA SEQUENCING
PLASMINOGEN-ACTIVATOR INHIBITOR TYPE-1 - REACTIVE CENTER AND AMINO-TERMINAL HETEROGENEITY DETERMINED BY PROTEIN AND CDNA SEQUENCING
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DOI：
10.1016/0014-5793(86)81113-9
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发表时间：
1986-12-15
期刊：
影响因子：
3.5
通讯作者：
DANO, K
中科院分区：
文献类型：
--
作者：
ANDREASEN, PA;RICCIO, A;DANO, K
尿激酶型和组织型纤溶酶原激活剂都可以将它们的5 × 4 kDa型1抑制剂（PAI‐1）转化为具有较低表观分子质量的无活性形式。我们测定了人类天然PAI‐1和转化PAI‐1的氨基末端氨基酸序列，分离了PAI‐1 cDNA，并测定了氨基酸末端和裂解位点对应区域的核苷酸序列。数据表明，抑制剂的转化包括从羧基端切割Arg - Met键33个残基，从而使抑制剂的反应中心定位在该位置。此外，在氨基端发现了异质性，Ser - Ala - Val - His - His形式和两残基短形式（Val - His - His -）的数量大致相等。
Both the urokinase‐type and tissue‐type plasminogen activator can convert their 5̃4 kDa type‐1 inhibitor (PAI‐1) to an inactive form with a lower apparent molecular mass. We have determined the amino‐terminal amino acid sequences of human native and converted PAI‐1, and isolated PAI‐1 cDNA and determined the nucleotide sequence in regions corresponding to the amino‐terminus and the cleavage site. The data show that the conversion of the inhibitor consists of cleavage of an Arg‐Met bond 33 residues from the carboxy‐terminus, thus localizing the reactive center of the inhibitor to that position. In addition, a heterogeneity was found at the amino‐terminus, with a Ser‐Ala‐Val‐His‐His form and a two‐residue shorter form (Val‐His‐His‐) occurring in approximately equal quantities.