Arylsulfatase a from normal human lung and lung tumors showed different patterns of microheterogeneity.

Arylsulfatase a from normal human lung and lung tumors showed different patterns of microheterogeneity. Research Abstract Details 

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Arylsulfatase a from normal human lung and lung tumors showed different patterns of microheterogeneity. Abstract Text:

M Nakamura,S Gasa,A Makita,

Arylsulfatase A was purified from human lung to apparent homogeneity as determined by electrophoresis in the presence of sodium dodecyl sulfate. The enzyme from normal lung as well as that from lung adenocarcinoma showed considerable microheterogeneity when examined by isoelectric focussing, with an isoelectric point (pI) ranging from 5.1 to 4.6. The tumor enzyme was more heterogeneous and contained more acidic components than the normal lung enzyme. The cause of the charge heterogeneity was examined by treatment with exogenous hydrolases. Upon treatment with sialidase, phosphatase or endo-beta-N-acetylglucosaminidase H (endoglycosidase H), the acidic enzyme forms shifted to an alkaline region on isoelectric focussing gels. Combined treatment of the arylsulfatase A with endoglycosidase H and sialidase resulted in complete loss of the most acidic components to give the less acidic components with pI 5.1, 5.0, and 4.9. These results strongly suggest that the charge heterogeneity of arylsulfatase A is due not only to sialylation but also to phosphorylation at the carbohydrate moiety of the enzyme, and the extent of substitution by acidic groups is markedly increased in the tumor enzyme.

Arylsulfatase a from normal human lung and lung tumors showed different patterns of microheterogeneity. Publishing Authors By Initials

M Nakamura,S Gasa,A Makita,

For similar enzymes and coenzymes: enzymes: hydrolases: esterases: sulfatases research abstracts see: enzymes and coenzymes: enzymes: hydrolases: esterases: sulfatases research

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Arylsulfatase a from normal human lung and lung tumors showed different patterns of microheterogeneity. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 96

Page Numbers: 207-13

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Jul

YEAR: 1984

Arylsulfatase a from normal human lung and lung tumors showed different patterns of microheterogeneity. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Arylsulfatase a from normal human lung and lung tumors showed different patterns of microheterogeneity. Keywords Mesh Terms:

KEYWORDS: Sulfatases

MESH TERMS: isolation & purification

Chemical & Substance for Abstract: Arylsulfatase a from normal human lung and lung tumors showed different patterns of microheterogeneity. Information

Substance Name: Mannosyl-Glycoprotein Endo-beta-N-Acetyl

Registry Number: EC 3.2.1.96

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Country: JAPAN

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MEDLINETA: J Biochem

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