RABBIT LIVER TRANSGLUTAMINASE - PHYSICAL, CHEMICAL, AND CATALYTIC PROPERTIES
RABBIT LIVER TRANSGLUTAMINASE - PHYSICAL, CHEMICAL, AND CATALYTIC PROPERTIES
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DOI：
10.1021/bi00644a016
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发表时间：
1977-01-01
期刊：
影响因子：
2.9
通讯作者：
FOLK, JE
中科院分区：
文献类型：
--
作者：
ABE, T;CHUNG, SI;FOLK, JE
转氨酶（R-谷氨酰-肽：胺α-谷氨酰-酰基转移酶[EC 2.3.2.13]）从兔肝提取物中纯化至表观均一性。该酶是一条约80，000 MW的单链多肽链，每个分子含有1个催化位点。分离的酶是充分表征的豚鼠肝转氨酶的兔对应物，这由它们的氨基酸组成和它们对几种底物的酶活性的相似性以及分离的兔酶在免疫学上不同于兔血浆和兔血小板凝血因子XIII的事实证明。兔酶和豚鼠酶的催化活性之间的显著差异是兔转氨酶对羟胺掺入苄氧羰基-L-精氨酸甘氨酸的低活性，豚鼠酶对该反应显示出高反应性。这一发现揭示了早期报道中的错误原因，即兔子肝脏中几乎不含这种酶。本文报道了本研究中使用的几种含谷氨酰胺的肽衍生物的制备和分析数据。
Transglutaminase (R-glutaminyl-peptide:amine .alpha.-glutamyl-yltransferase [EC 2.3.2.13]) was purified to apparent homogeneity from extracts of rabbit liver. The enzyme is a single polypeptide chain of approximately 80,000 MW containing 1 catalytic site per molecule. That the isolated enzyme is the rabbit counterpart of the well-characterized guinea pig liver transglutaminase is evidenced by the similarities in their amino acid compositions and in their enzymic activities toward several substrates, together with the fact that the isolated rabbit enzyme is immunologically distinct from both rabbit plasma and rabbit platelet blood coagulation factor XIII. A striking difference between the catalytic activities of the rabbit and guinea pig enzymes is the low activity of rabbit transglutaminase for hydroxylamine incorporation into benzyloxycarbonyl-L-glutaminylglycine, a reaction for which the guinea pig enzyme shows a high reactivity. This finding reveals the cause of error in an earlier report that rabbit liver contains little, if any, of the enzyme. Preparation of, and analytical data on, several glutamine-containing peptide derivatives used in this study are reported here.