Literature DB >> 5861842

A low molecular-weight form of urease.

P P Seghal, R J Tanis, A W Naylor.   

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Year:  1965        PMID： 5861842     DOI： 10.1016/0006-291x(65)90433-x

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN： 0006-291X            Impact factor:   3.575


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  7 in total

1.  Microbial L-phenylalanine ammonia-lyase. Purification, subunit structure and kinetic properties of the enzyme from Rhizoctonia solani.

Authors:  K K Kalghatgi; P V Subba Rao
Journal:  Biochem J       Date:  1975-07       Impact factor: 3.857

2.  Radiation-target molecular weights of urease and of L-glutamate dehydrogenase, and their relevance to the size of the functional subunits.

Authors:  E Blum; T Alper
Journal:  Biochem J       Date:  1971-05       Impact factor: 3.857

3.  Dissociation of urease in acetate buffer of pH 3.5 with retention of the enzymatic activity.

Authors:  G Gorin; C C Chin; S F Wang
Journal:  Experientia       Date:  1968-07-15

4.  Purification and comparative properties of microsomal and glyoxysomal malate synthase from castor bean endosperm.

Authors:  L Bowden; J M Lord
Journal:  Plant Physiol       Date:  1978-02       Impact factor: 8.340

5.  Urease. 8. Its interaction with sodium dodecyl sulfate.

Authors:  G Gorin; G Mamiya; C C Chin
Journal:  Experientia       Date:  1967-06-15

6.  Physical and chemical studies of a low-molecular-weight form of urease.

Authors:  R J Tanis; A W Naylor
Journal:  Biochem J       Date:  1968-08       Impact factor: 3.857

7.  Degradation of (+/-)-synephrine by Arthrobacter synephrinum. Oxidation of 3,4-dihydroxyphenylacetate to 2-hydroxy-5-carboxymethyl-muconate semialdehyde.

Authors:  R K Kutty; N A Devi; M Veeraswamy; S Ramesh; P V Rao
Journal:  Biochem J       Date:  1977-10-01       Impact factor: 3.857
  7 in total

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