Immobilized Glucuronosyltransferase for the Synthesis of Conjugates

Indu Parikh; Donald W. MacGlashan; Catherine Fenselau

doi:10.1021/jm00224a018

Immobilized Glucuronosyltransferase for the Synthesis of Conjugates

Indu Parikh, Donald W. MacGlashan, Catherine Fenselau

School of Medicine

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

33 Scopus citations

Abstract

Partially purified rabbit liver UDPglucuronosyltransferase is immobilized on agarose by the cyanogen bromide activation method. Both soluble and matrix-bound enzyme preparations display very similar K_m and pH optimum. The storage stability of the immobilized enzyme at 4° is 5-10 times improved over the soluble preparations. The agarose-bound UDPglucuronosyltransferase is successfully used in the synthesis of p-nitrophenyl glucuronide in an overall yield of 50-70%. The matrix-bound enzyme is reusable over an extended period of time and offers an easy and convenient synthetic tool for various drug glucuronides.

Original language	English (US)
Pages (from-to)	296-299
Number of pages	4
Journal	Journal of medicinal chemistry
Volume	19
Issue number	2
DOIs	https://doi.org/10.1021/jm00224a018
State	Published - Feb 1 1976

ASJC Scopus subject areas

Molecular Medicine
Drug Discovery

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10.1021/jm00224a018

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abstract = "Partially purified rabbit liver UDPglucuronosyltransferase is immobilized on agarose by the cyanogen bromide activation method. Both soluble and matrix-bound enzyme preparations display very similar Km and pH optimum. The storage stability of the immobilized enzyme at 4° is 5-10 times improved over the soluble preparations. The agarose-bound UDPglucuronosyltransferase is successfully used in the synthesis of p-nitrophenyl glucuronide in an overall yield of 50-70%. The matrix-bound enzyme is reusable over an extended period of time and offers an easy and convenient synthetic tool for various drug glucuronides.",

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AU - MacGlashan, Donald W.

AU - Fenselau, Catherine

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N2 - Partially purified rabbit liver UDPglucuronosyltransferase is immobilized on agarose by the cyanogen bromide activation method. Both soluble and matrix-bound enzyme preparations display very similar Km and pH optimum. The storage stability of the immobilized enzyme at 4° is 5-10 times improved over the soluble preparations. The agarose-bound UDPglucuronosyltransferase is successfully used in the synthesis of p-nitrophenyl glucuronide in an overall yield of 50-70%. The matrix-bound enzyme is reusable over an extended period of time and offers an easy and convenient synthetic tool for various drug glucuronides.

AB - Partially purified rabbit liver UDPglucuronosyltransferase is immobilized on agarose by the cyanogen bromide activation method. Both soluble and matrix-bound enzyme preparations display very similar Km and pH optimum. The storage stability of the immobilized enzyme at 4° is 5-10 times improved over the soluble preparations. The agarose-bound UDPglucuronosyltransferase is successfully used in the synthesis of p-nitrophenyl glucuronide in an overall yield of 50-70%. The matrix-bound enzyme is reusable over an extended period of time and offers an easy and convenient synthetic tool for various drug glucuronides.

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Immobilized Glucuronosyltransferase for the Synthesis of Conjugates

Abstract

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