ALPHA-1-ANTITRYPSIN CHRISTCHURCH, 363 GLU-] LYS - MUTATION AT THE P5' POSITION DOES NOT AFFECT INHIBITORY ACTIVITY
ALPHA-1-ANTITRYPSIN CHRISTCHURCH, 363 GLU-] LYS - MUTATION AT THE P5' POSITION DOES NOT AFFECT INHIBITORY ACTIVITY
复制标题
DOI：
10.1016/0167-4838(86)90183-4
复制
发表时间：
1986-09-05
期刊：
影响因子：
--
通讯作者：
CARRELL, RW
中科院分区：
文献类型：
--
作者：
BRENNAN, SO;CARRELL, RW
从一名柬埔寨妇女的血浆中分离出α 1-抗胰蛋白酶基督城，该妇女对于该变体和正常M蛋白是杂合的。胰蛋白酶肽图谱显示，359-365 Ser-Ile-Pro-Pro-Glu，瓦尔，Lys的构象位点肽缺失，并被两个新的肽Ser-Ile-Pro-Pro，Lys和Val-Lys取代，表明363 Glu →的突变。里斯没有与这种新的抗胰蛋白酶相关的明显临床症状。竞争实验表明，抗胰蛋白酶基督城反应在相同的速率正常抗胰蛋白酶的存在下，有限数量的胰蛋白酶，糜蛋白酶，凝血酶和中性粒细胞弹性蛋白酶。这两种抑制剂被催化量的木瓜蛋白酶灭活。这种失活是由于在P7位置的苯丙氨酸残基处的裂解，即朝向抑制位点的N-末端的7个残基。描述了一种用于分离木瓜蛋白酶裂解产物的一步乙醇提取程序。
.alpha.1-Antitrypsin Christchurch was isolated from the plasma of a Cambodian woman who was heterozygous for this variant and for the normal M protein. Tryptic peptide maps revealed that the inhibitory-site peptide, 359-365 Ser-Ile-Pro-Pro-Glu,Val,Lys, was missing and replaced by two new peptides Ser-Ile-Pro-Pro,Lys and Val-Lys, indicating a mutation of 363 Glu .fwdarw. Lys. There was no obvious clinical condition associated with this new antitrypsin. Competition experiments showed that antitrypsin Christchurch reacted at the same rate as normal antitrypsin in the presence of limiting amounts of trypsin, chymotrypsin, thrombin and neutrophil elastase. Both inhibitors were inactivated by catalytic amounts of papain. This inactivation was due to cleavage at the phenylalanine residue at the P7 position, seven residues towards the N-terminal of the inhibitory site. A one-step ethanol extraction procedure is described for isolating the papain cleavage products.