Photoregulation of the Activities of Proteins

Shai Rubin; Itamar Willner

doi:10.1080/10587259408037814

Photoregulation of the Activities of Proteins

Shai Rubin
, Itamar Willner

Institute of Chemistry

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

3 Scopus citations

Abstract

Azobenzene modified papain, reveals photoregulation toward hydrolysis of Nα-benzoyl-DL-arginine-4-mtroanilide. The association constants of thiophenefulgide modified concanavolin A (Con. A) towards monosaccharides is reversibly photoregulated. Immobilized α-chymotrypsin in photochromic copolymers exhibits “ON-OFF” photoregulation towards the hydrolysis of N-(3-carboxpropionyl)-L-phenylalanine p-nitroanilide.

Original language	English
Pages (from-to)	201-205
Number of pages	5
Journal	Molecular Crystals and Liquid Crystals
Volume	246
Issue number	1
DOIs	https://doi.org/10.1080/10587259408037814
State	Published - 1 May 1994

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title = "Photoregulation of the Activities of Proteins",

abstract = "Azobenzene modified papain, reveals photoregulation toward hydrolysis of Nα-benzoyl-DL-arginine-4-mtroanilide. The association constants of thiophenefulgide modified concanavolin A (Con. A) towards monosaccharides is reversibly photoregulated. Immobilized α-chymotrypsin in photochromic copolymers exhibits “ON-OFF” photoregulation towards the hydrolysis of N-(3-carboxpropionyl)-L-phenylalanine p-nitroanilide.",

author = "Shai Rubin and Itamar Willner",

year = "1994",

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AB - Azobenzene modified papain, reveals photoregulation toward hydrolysis of Nα-benzoyl-DL-arginine-4-mtroanilide. The association constants of thiophenefulgide modified concanavolin A (Con. A) towards monosaccharides is reversibly photoregulated. Immobilized α-chymotrypsin in photochromic copolymers exhibits “ON-OFF” photoregulation towards the hydrolysis of N-(3-carboxpropionyl)-L-phenylalanine p-nitroanilide.

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Photoregulation of the Activities of Proteins

Abstract

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