Purification and properties of five different forms of human procarboxypeptidases - Wikidata - wikimedia - TriplyDB

Purification and properties of five different forms of human procarboxypeptidases

Purification and properties of five different forms of human procarboxypeptidases

http://www.wikidata.org/entity/Q24294259

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cDNA cloning and sequence analysis of human pancreatic procarboxypeptidase A1 The three-dimensional structure of human procarboxypeptidase A2. Deciphering the basis of the inhibition, activation and intrinsic activity of the zymogen A novel carboxypeptidase B that processes native beta-amyloid precursor protein is present in human hippocampus Further studies on the human pancreatic binary complexes involving procarboxypeptidase A Cloning, sequencing and functional expression of a cDNA encoding porcine pancreatic preprocarboxypeptidase A1.Inactivation of active thrombin-activable fibrinolysis inhibitor takes place by a process that involves conformational instability rather than proteolytic cleavage.Heterologous microarray experiments used to identify the early gene response to heat stress in a coral reef fish.The sequence and conformation of human pancreatic procarboxypeptidase A2. cDNA cloning, sequence analysis, and three-dimensional model.Characterisation and preliminary X-ray diffraction analysis of human pancreatic procarboxypeptidase A2.Chymotrypsin C is a co-activator of human pancreatic procarboxypeptidases A1 and A2.Identification of a procarboxypeptidase A-truncated protease E binary complex in human pancreatic juice.The proteasome: a macromolecular assembly designed to confine proteolysis to a nanocompartment.Genetic Analysis of Human Chymotrypsin-Like Elastases 3A and 3B (CELA3A and CELA3B) to Assess the Role of Complex Formation between Proelastases and Procarboxypeptidases in Chronic Pancreatitis.Complex Formation of Human Proelastases with Procarboxypeptidases A1 and A2.Distribution of manganese in rat pancreas and identification of its primary binding protein as pro-carboxypeptidase B.Comparative analysis of the sequences and three-dimensional models of human procarboxypeptidases A1, A2 and B.Autolysis of proproteinase E in bovine procarboxypeptidase A ternary complex gives rise to subunit III.Mapping the pro-region of carboxypeptidase B by protein engineering. Cloning, overexpression, and mutagenesis of the porcine proenzyme.Overexpression of Human Procarboxypeptidase A2 inPichia pastorisand Detailed Characterization of Its Activation Pathway Crystallization and preliminary X-ray analysis of the ternary complex of procarboxypeptidase A from bovine pancreas

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P2860

Purification and properties of five different forms of human procarboxypeptidases

http://www.wikidata.org/entity/Q24294259

description

1989 nî lūn-bûn

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1989 թուականի Փետրուարին հրատարակուած գիտական յօդուած

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1989 թվականի փետրվարին հրատարակված գիտական հոդված

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1989年の論文

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1989年論文

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1989年論文

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1989年論文

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1989年論文

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1989年論文

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1989年论文

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name

Purification and properties of five different forms of human procarboxypeptidases

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Purification and properties of five different forms of human procarboxypeptidases

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Purification and properties of five different forms of human procarboxypeptidases

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Purification and properties of five different forms of human procarboxypeptidases

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Purification and properties of five different forms of human procarboxypeptidases

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Purification and properties of five different forms of human procarboxypeptidases

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Purification and properties of five different forms of human procarboxypeptidases

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Purification and properties of five different forms of human procarboxypeptidases

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Purification and properties of five different forms of human procarboxypeptidases

@ast

Purification and properties of five different forms of human procarboxypeptidases

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Purification and properties of five different forms of human procarboxypeptidases

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Purification and properties of five different forms of human procarboxypeptidases

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P1476

Purification and properties of five different forms of human procarboxypeptidases

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E Mendez

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F J Burgos

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P2860

Purification of carboxypeptidase B from human pancreas

A novel proteinase from human pancreas.

Preparative isolation of the two forms of pig pancreatic pro-(carboxypeptidase A) and their monomeric carboxypeptidases A

Comparison between the monomeric and binary-complex forms of procarboxypeptidase A from whole pig pancreas.

Isolation and re-association of the subunits from the pro-(carboxypeptidase A)-pro-(proteinase E) binary complex from pgi pancreas.

Pro-(carboxypeptidases A) from whole pig pancreas. Their mass, size, shape and solvation.

Effect of temperature upon the conformations of carboxypeptidase A (Anson), A gamma Leu, A gamma Val, AND A alpha + beta.

Urea-gradient gel electrophoresis studies on the association of procarboxypeptidases A and B, proproteinase E, and their tryptic activation products

The severed activation segment of porcine pancreatic procarboxypeptidase a is a powerful inhibitor of the active enzyme Isolation and characterisation of the activation peptide

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609-16

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scholarly article

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10.1111/J.1432-1033.1989.TB14590.X

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P433

3

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2920728

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P921

zinc ion binding

Carboxypeptidase A2

Carboxypeptidase A1