雪貂泌乳乳腺胆盐依赖性脂肪酶的分子克隆:功能残基综述

Véronique Sbarra , Nadine Bruneau , Eric Mas , Margit Hamosh , Dominique Lombardo , Paul Hamosh
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引用次数: 18

摘要

利用RT-PCR技术克隆了雪貂泌乳乳腺胆汁盐依赖性脂肪酶(BSDL, EC 3.1.1.-)。开放阅读框由1869个核苷酸组成,编码该功能酶的623个氨基酸。与其他物种相比,在残基1和484之间的同源性最大,在相似序列的7个重复片段所在的c端几乎没有同源性。与其他乳汁或胰腺BSDL相比,雪貂乳腺BSDL在类似位置保留了活性位点和肝素结合位点的残基。其他重要的项目,如肽与伴侣分子的结合,磷酸化位点或胆盐结合位点,也初步定位在7个可用的BSDL序列的良好保守区域。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Molecular cloning of the bile salt-dependent lipase of ferret lactating mammary gland: an overview of functional residues

Ferret lactating mammary gland bile salt-dependent lipase (BSDL, EC 3.1.1.-) has been cloned by RT-PCR. The open reading frame consists of 1869 nucleotides which encode 623 amino acids of the functional enzyme. When compared to other species, the greatest homology is observed between residues 1 and 484, with little or no homology at the C-terminal end where seven repeated segments of similar sequence are located. Ferret mammary gland BSDL retains residues involved in the active site and the tentative heparin binding site at similar positions in comparison to other milk or pancreatic BSDL. Other important items, such as binding peptide to chaperone molecular, phosphorylation site(s) or bile salt binding sites, were also tentatively located in well conserved regions of seven available BSDL sequences.

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