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猪羧肽酶原A激活片段的构象及配体结合特性分析

Analysis of the conformation and ligand-binding properties of the activation segment of pig procarboxypeptidase A.

作者信息

Vilanova M, Vendrell J, Cuchillo C M, Avilés F X

机构信息

Departament de Bioquimica i Biologia Molecular (Unitat de Ciències), Universitat Autònoma de Barcelona, Spain.

出版信息

Biochem J. 1988 May 1;251(3):901-5. doi: 10.1042/bj2510901.

DOI:10.1042/bj2510901
PMID:2458099
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1149087/
Abstract

The isolated activation segment of pig procarboxypeptidase A binds two Tb3+ ions in a strong and specific way. In contrast, the binding of Ca2+, Cd2+ and Mg2+ is weak. The binding of Tb3+ increases the resistance of the isolated activation segment against proteolysis and competes for the binding of the carbocyanine dye Stains-All. This dye forms complexes with the activation segment showing spectral properties similar to those observed with EF-hand structures. The presented results support a previous hypothesis on the existence of two regions in the activation segment of pancreatic procarboxypeptidases structurally related to Ca2+-binding domains of the EF-hand protein family.

摘要

猪羧肽酶原A的分离活化片段以强烈且特异的方式结合两个Tb3+离子。相比之下，Ca2+、Cd2+和Mg2+的结合较弱。Tb3+的结合增加了分离活化片段对蛋白水解的抗性，并竞争羰花青染料Stains-All的结合。这种染料与活化片段形成复合物，其光谱特性与在EF-手结构中观察到的相似。所呈现的结果支持了先前的一个假设，即在胰腺羧肽酶原的活化片段中存在两个区域，其结构与EF-手蛋白家族的Ca2+结合域相关。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0998/1149087/ebd50af338af/biochemj00232-0268-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0998/1149087/ebd50af338af/biochemj00232-0268-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0998/1149087/ebd50af338af/biochemj00232-0268-a.jpg

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本文引用的文献

1
Effects of cations on affinity of calmodulin for calcium: ordered binding of calcium ions allows the specific activation of calmodulin-stimulated enzymes.阳离子对钙调蛋白与钙亲和力的影响：钙离子的有序结合可使钙调蛋白刺激的酶特异性激活。
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The activation segment of procarboxypeptidase A from porcine pancreas constitutes a folded structural domain.
FEBS Lett. 1982 Nov 29;149(2):257-60. doi: 10.1016/0014-5793(82)81112-5.
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The severed activation segment of porcine pancreatic procarboxypeptidase A is a powerful inhibitor of the active enzyme. Isolation and characterisation of the activation peptide.猪胰蛋白酶原A的切割激活片段是活性酶的强效抑制剂。激活肽的分离与鉴定。
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Pro-(carboxypeptidases A) from whole pig pancreas. Their mass, size, shape and solvation.来自全猪胰腺的羧肽酶A原。它们的质量、大小、形状和溶剂化作用。
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Luminescence and circular-dichroism analysis of terbium binding by pig intestinal calcium-binding protein (relative mass = 9000).
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Evolution of proteolytic enzymes.蛋白水解酶的进化
Science. 1984 Apr 27;224(4647):350-7. doi: 10.1126/science.6369538.
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Calcium binding domains of calmodulin. Sequence of fill as determined with terbium luminescence.钙调蛋白的钙结合结构域。用铽发光测定的填充序列。
J Biol Chem. 1982 Feb 25;257(4):1845-54.