Literature DB >> 4447621

Purification of alpha-mannosidase from jack-bean meal suitable for use as reagent.

C Y Chu, M D Turner.   

Abstract

A simple method of purification of alpha-mannosidase from jack-bean meal is described which yields a product free of beta-N-acetylglucosaminidase activity.

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Year:  1974        PMID： 4447621      PMCID： PMC1166304          DOI： 10.1042/bj1390469

Source DB:  PubMed          Journal:  Biochem J        ISSN： 0264-6021            Impact factor:   3.857


  4 in total

1.  Studies on the glycosidases in jack bean meal. I. Isolation and properties of alpha-mannosidase.

Authors:  Y T Li
Journal:  J Biol Chem       Date:  1967-12-10       Impact factor: 5.157

2.  A nomogram for ammonium sulphate solutions.

Authors:  M DIXON
Journal:  Biochem J       Date:  1953-06       Impact factor: 3.857

3.  Protein measurement with the Folin phenol reagent.

Authors:  O H LOWRY; N J ROSEBROUGH; A L FARR; R J RANDALL
Journal:  J Biol Chem       Date:  1951-11       Impact factor: 5.157

4.  Presence of alpha-D-mannosidic linkage in glycoproteins. Liberation of d-mannose from various glycoproteins by alpha-mannosidase isolated from jack bean meal.

Authors:  Y T Li
Journal:  J Biol Chem       Date:  1966-02-25       Impact factor: 5.157
  4 in total
  1 in total

1.  The homology of the major storage protein of jack bean (Canavalia ensiformis) to pea vicilin and its separation from α-mannosidase.

Authors:  R H Sammour; J A Gatehouse; J Gilroy; D Boulter
Journal:  Planta       Date:  1984-01       Impact factor: 4.116
  1 in total

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