Functional properties of beta-galactosidase from mutant strain 13 PO of Escherichia coli. - Wikidata - wikimedia - TriplyDB

Functional properties of beta-galactosidase from mutant strain 13 PO of Escherichia coli.

Functional properties of beta-galactosidase from mutant strain 13 PO of Escherichia coli.

http://www.wikidata.org/entity/Q37584049

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Functional properties of beta-galactosidase from mutant strain 13 PO of Escherichia coli.

http://www.wikidata.org/entity/Q37584049

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on April 1978

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Functional properties of beta-galactosidase from mutant strain 13 PO of Escherichia coli.

@en

Functional properties of beta-galactosidase from mutant strain 13 PO of Escherichia coli.

@nl

type

label

Functional properties of beta-galactosidase from mutant strain 13 PO of Escherichia coli.

@en

Functional properties of beta-galactosidase from mutant strain 13 PO of Escherichia coli.

@nl

prefLabel

Functional properties of beta-galactosidase from mutant strain 13 PO of Escherichia coli.

@en

Functional properties of beta-galactosidase from mutant strain 13 PO of Escherichia coli.

@nl

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Functional properties of beta-galactosidase from mutant strain 13 PO of Escherichia coli.

@en

P2093

Deschavanne PJ

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Viratelle OM

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Yon JM

http://www.w3.org/2001/XMLSchema#string

P2860

The determination of the concentration of hydrolytic enzyme solutions: alpha-chymotrypsin, trypsin, papain, elastase, subtilisin, and acetylcholinesterase

The amino acid sequence of beta-galactosidase of Escherichia coli

Genetic evidence for the disposition of the substrate binding site of beta-galactosidase.

The statistical analysis of enzyme kinetic data.

The mechanism of action of beta-galactosidase. Effect of aglycone nature and -deuterium substitution on the hydrolysis of aryl galactosides.

[Nucleophilic competition in enzymic hydrolytic reactions. Kinetic analysis and application to the tryptic hydrolysis of some esters].

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1892-1896

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scholarly article

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10.1073/PNAS.75.4.1892

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4

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75

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1978-04-01T00:00:00Z

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23109076

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25441

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392447

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