A micro-scale method for the conjugation of affinity-purified Fab' to beta-D-galactosidase from Escherichia coli.

A micro-scale method for the conjugation of affinity-purified Fab' to beta-D-galactosidase from Escherichia coli. Research Abstract Details 

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A micro-scale method for the conjugation of affinity-purified Fab' to beta-D-galactosidase from Escherichia coli. Abstract Text:

S Inoue,S Hashida,T Kohno,K Tanaka,E Ishikawa,

A micro-scale method for the conjugation of affinity-purified Fab' to beta-D-galactosidase from Escherichia coli is described. Rabbit anti-human chorionic gonadotropin serum (0.2 ml) was digested with pepsin to convert IgG to F(ab')2 and applied to a column of human chorionic gonadotropin-Sepharose 4B, followed by elution at pH 2.5. The affinity-purified anti-human chorionic gonadotropin F(ab')2 was mixed with non-specific goat F(ab')2 (0.5 mg) as a carrier, reduced with 2-mercaptoethylamine to split F(ab')2 to Fab' and conjugated to beta-D-galactosidase using N,N'-o-phenylenedimaleimide. The affinity-purified rabbit anti-human chorionic gonadotropin Fab'-beta-D-galactosidase conjugate was separated from non-specific goat Fab'-beta-D-galactosidase conjugate and unconjugated beta-D-galactosidase by affinity chromatography on a column of goat (anti-rabbit IgG) IgG-Sepharose 4B using 4 M urea. The amount of the affinity-purified conjugate obtained was 56-69 micrograms. The detection limit of human chorionic gonadotropin by a sandwich enzyme immunoassay technique was improved 30-fold by using the affinity-purified conjugate as compared with that before affinity-purification. This method is applicable to the conjugation with alkaline phosphatase from calf intestine and probably also other enzymes which are stable in 4 M urea.

A micro-scale method for the conjugation of affinity-purified Fab' to beta-D-galactosidase from Escherichia coli. Publishing Authors By Initials

S Inoue,S Hashida,T Kohno,K Tanaka,E Ishikawa,

For similar biochemical phenomena, metabolism, and nutrition: biochemical phenomena: protein binding research abstracts see: biochemical phenomena, metabolism, and nutrition: biochemical phenomena: protein binding research

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A micro-scale method for the conjugation of affinity-purified Fab' to beta-D-galactosidase from Escherichia coli. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biochemistry

VOLUME: 98

Page Numbers: 1387-94

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Nov

YEAR: 1985

A micro-scale method for the conjugation of affinity-purified Fab' to beta-D-galactosidase from Escherichia coli. Information

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LANGUAGE: eng

NlmUniqueID: 376600

A micro-scale method for the conjugation of affinity-purified Fab' to beta-D-galactosidase from Escherichia coli. Keywords Mesh Terms:

KEYWORDS: Protein Binding

MESH TERMS: isolation & purification

Chemical & Substance for Abstract: A micro-scale method for the conjugation of affinity-purified Fab' to beta-D-galactosidase from Escherichia coli. Information

Substance Name: Galactosidases

Registry Number: EC 3.2.1.-

Grant and Affiliation Information for A micro-scale method for the conjugation of affinity-purified Fab' to beta-D-galactosidase from Escherichia coli.

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Country: JAPAN

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MEDLINETA: J Biochem

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