Literature DB >> 36034

The monomer -- dimer association of rabbit lver aryl sulfatase A and its relationship to the anomalous kinetics.

A Waheed, R L Van Etten.   

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Year:  1979        PMID： 36034     DOI： 10.1016/0003-9861(79)90612-x

Source DB:  PubMed          Journal:  Arch Biochem Biophys        ISSN： 0003-9861            Impact factor:   4.013


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  5 in total

1.  Four monoclonal antibodies inhibit the recognition of arylsulphatase A by the lysosomal enzyme phosphotransferase.

Authors:  H J Sommerlade; A Hille-Rehfeld; K von Figura; V Gieselmann
Journal:  Biochem J       Date:  1994-01-01       Impact factor: 3.857

Review 2.  The anomalous kinetics of sulphatase A.

Authors:  A B Roy; T J Mantle
Journal:  Biochem J       Date:  1989-08-01       Impact factor: 3.857

3.  The slow kinetic transients of arylsulphatase A.

Authors:  C O'Fagain; U Bond; B A Orsi; T J Mantle
Journal:  Biochem J       Date:  1982-02-01       Impact factor: 3.857

4.  Driving forces of protein association: the dimer-octamer equilibrium in arylsulfatase A.

Authors:  Peter Vagedes; Wolfram Saenger; Ernst-Walter Knapp
Journal:  Biophys J       Date:  2002-12       Impact factor: 4.033

5.  Isolation and characterization of the pig endometrial arylsulphatase A.

Authors:  H Rahi; P N Srivastava
Journal:  Biochem J       Date:  1983-06-01       Impact factor: 3.857
  5 in total

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