Mechanism of proteinase complex formation with alpha 2-macroglobulin. Three modes of trypsin binding (Q72644079)

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28 October 2019

title

Mechanism of proteinase complex formation with alpha 2-macroglobulin. Three modes of trypsin binding (English)

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28 October 2019

author name string

Sottrup-Jensen L

series ordinal

1

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28 October 2019

Petersen TE

series ordinal

2

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28 October 2019

Magnusson S

series ordinal

3

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28 October 2019

publication date

1 June 1981

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28 October 2019

number of pages

6

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based on heuristic

inferred from page(s)

published in

FEBS Letters

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28 October 2019

volume

128

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28 October 2019

issue

1

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28 October 2019

page(s)

127-132

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Studies on human plasma alpha 2-macroglobulin-enzyme interactions. Evidence for proteolytic modification of the subunit chain structure

28 October 2019

cites work

1 reference

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The interaction of alpha 2-macroglobulin with proteinases. Characteristics and specificity of the reaction, and a hypothesis concerning its molecular mechanism

21 January 2018

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The interaction of alpha2-macroglobulin with proteinases. Binding and inhibition of mammalian collagenases and other metal proteinases

21 January 2018

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Protein binding of pancreatic proteolytic enzymes

21 January 2018

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MACROGLOBULIN FROM HUMAN PLASMA WHICH FORMS AN ENZYMATICALLY ACTIVE COMPOUND WITH TRYPSIN

21 January 2018

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Determination of alpha-2-macroglobulin as trypsin-protein esterase

21 January 2018

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Physical and chemical properties of human plasma β2-macroglobulin

21 January 2018

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The electrophoretically ‘slow’ and ‘fast’ forms of the α2-macroglobulin molecule

21 January 2018

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Primary structure of the 'bait' region for proteinases in alpha 2-macroglobulin. Nature of the complex

21 January 2018

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The identification of distinctive forms of human α2-macroglobulin by using the numerical relationship between trypsin binding in α- and β-modes

21 January 2018

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A thiol-ester in α2-macroglobulin cleaved during proteinase complex formation

21 January 2018

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Sequence location of the reactive thiol ester in human alpha 2-macroglobulin

21 January 2018

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Characterization of alkylamine-sensitive site in alpha 2-macroglobulin

21 January 2018

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Trypsin-induced activation of the thiol esters in α2-macroglobulin generates a short-lived intermediate (‘nascent’ α2M) that can react rapidly to incorporate not only methylamine or putrescine but also proteins lacking proteinase activity

21 January 2018

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Third component of human complement: structural requirements for its function

21 January 2018

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Evidence for presence of an internal thiolester bond in third component of human complement.

21 January 2018

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Relation of putative thioester bond in C3 to activation of the alternative pathway and the binding of C3b to biological targets of complement

21 January 2018

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The covalent-binding reaction of complement component C3

21 January 2018

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The binding of human complement component C4 to antibody-antigen aggregates

21 January 2018

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Covalent binding of proteinases in their reaction with α2-macroglobulin

21 January 2018

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Binding of anhydrotrypsin to α2-macroglobulin

21 January 2018

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Isolation of trypsins by affinity chromatography

21 January 2018

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Preparation of Iodine-131 Labelled Human Growth Hormone of High Specific Activity

21 January 2018

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Thiol reduction of human α2-macroglobulin. The subunit structure

21 January 2018

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Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. II. Crystallographic refinement at 1.9 A resolution.

21 January 2018

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Crystal structure of the complex of porcine trypsin with soybean trypsin inhibitor (Kunitz) at 2.6 Å resolution

21 January 2018

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The combining ratio between trypsin and serum alpha-2-macroglobulin

21 January 2018

1 reference

31 May 2024

https://opencitations.net/index/api/v1/citations/10.3891/ACTA.CHEM.SCAND.20-2299

Identifiers

DOI

10.1016/0014-5793(81)81097-6

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:6168492%20AND%20SRC:MED&resulttype=core&format=json

28 October 2019

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