Immobilized arylsulfotransferase

Dong Hyun Kim; Kyoichi Kobashi

doi:10.1093/oxfordjournals.jbchem.a122080

Immobilized arylsulfotransferase

Dong Hyun Kim, Kyoichi Kobashi

Research output: Contribution to journal › Article › peer-review

2 Citations (Scopus)

Abstract

Arylsulfotransferase was stabilized for storage more markedly by covalent immobilization onto AH-Sepharose-4B or CH-Sepharose -4B with EDC than by adsorptive immobilization onto DEAE-cellulose or DEAE-Sephadex. The optimal pH, K_m for sulfate donor and thermostability of covalently immobilized arylsulfotransferase were similar to those of the free enzyme. Tyrosine-containing peptides such as cholecytokinin-8-nonsulfate, tyrosine methylester and (Leu)enkephalin as acceptor substrates were effectively sulfated by the immobilized enzyme.

Original language	English
Pages (from-to)	487-491
Number of pages	5
Journal	Journal of Biochemistry
Volume	102
Issue number	3
DOIs	https://doi.org/10.1093/oxfordjournals.jbchem.a122080
Publication status	Published - Sep 1987

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title = "Immobilized arylsulfotransferase",

abstract = "Arylsulfotransferase was stabilized for storage more markedly by covalent immobilization onto AH-Sepharose-4B or CH-Sepharose -4B with EDC than by adsorptive immobilization onto DEAE-cellulose or DEAE-Sephadex. The optimal pH, Km for sulfate donor and thermostability of covalently immobilized arylsulfotransferase were similar to those of the free enzyme. Tyrosine-containing peptides such as cholecytokinin-8-nonsulfate, tyrosine methylester and (Leu)enkephalin as acceptor substrates were effectively sulfated by the immobilized enzyme.",

author = "Kim, {Dong Hyun} and Kyoichi Kobashi",

year = "1987",

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doi = "10.1093/oxfordjournals.jbchem.a122080",

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T1 - Immobilized arylsulfotransferase

AU - Kim, Dong Hyun

AU - Kobashi, Kyoichi

PY - 1987/9

Y1 - 1987/9

N2 - Arylsulfotransferase was stabilized for storage more markedly by covalent immobilization onto AH-Sepharose-4B or CH-Sepharose -4B with EDC than by adsorptive immobilization onto DEAE-cellulose or DEAE-Sephadex. The optimal pH, Km for sulfate donor and thermostability of covalently immobilized arylsulfotransferase were similar to those of the free enzyme. Tyrosine-containing peptides such as cholecytokinin-8-nonsulfate, tyrosine methylester and (Leu)enkephalin as acceptor substrates were effectively sulfated by the immobilized enzyme.

AB - Arylsulfotransferase was stabilized for storage more markedly by covalent immobilization onto AH-Sepharose-4B or CH-Sepharose -4B with EDC than by adsorptive immobilization onto DEAE-cellulose or DEAE-Sephadex. The optimal pH, Km for sulfate donor and thermostability of covalently immobilized arylsulfotransferase were similar to those of the free enzyme. Tyrosine-containing peptides such as cholecytokinin-8-nonsulfate, tyrosine methylester and (Leu)enkephalin as acceptor substrates were effectively sulfated by the immobilized enzyme.

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U2 - 10.1093/oxfordjournals.jbchem.a122080

DO - 10.1093/oxfordjournals.jbchem.a122080

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SP - 487

EP - 491

JO - Journal of Biochemistry

JF - Journal of Biochemistry

SN - 0021-924X

IS - 3

ER -

Immobilized arylsulfotransferase

Abstract

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