Literature DB >> 6146317

Microheterogeneity of arylsulfatase a: Treatment with hydrolytic enzymes.

T A Sarafian, A L Fluharty, H Kihara.   

Abstract

Cerebroside sulfatase also known as arylsulfatase A from human liver displays six microheteromer bands upon narrow pH range isoelectric focusing. Sialic acid residues only partially account for this enzyme multiplicity since neuraminidase treatment reduces the number of bands to three. Uptake studies with cultured fibroblasts strongly suggest arylsulfatase A has covalently bound mannose 6-phosphate residues. However, treatment with alkaline phosphatase and a battery of glycohydrolases failed to reduce the number of enzyme charge forms below three. These results imply that the neuraminidase-resistant charge microheterogeneity is not due to structures associated with the carbohydrate moiety of arylsulfatase A.

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Year:  1984        PMID: 6146317     DOI: 10.1016/0006-2944(84)90062-0

Source DB:  PubMed          Journal:  Biochem Med        ISSN: 0006-2944


  2 in total

1.  Attenuated activities and structural alterations of arylsulfatase A in tissues from subjects with pseudo arylsulfatase A deficiency.

Authors:  H Kihara; W E Meek; A L Fluharty
Journal:  Hum Genet       Date:  1986-09       Impact factor: 4.132

2.  The structural basis for the electrophoretic isoforms of normal and variant human platelet arylsulphatase A.

Authors:  R D Poretz; R S Yang; B Canas; H Lackland; S Stein; P Manowitz
Journal:  Biochem J       Date:  1992-11-01       Impact factor: 3.857

  2 in total

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