Purification of rat liver arylsulfatase A and its microheterogenity assayed by crossed affinity-immunoelectrophoresis

• Autorzy: Wojczyk B. , Hoja D. , Litynska A.
• Języki publikacji: EN

Abstrakty

EN

Arylsulfatase A (arylsulfatase sulfohydrolase) EC 3.1.6*1 was purified from rat liver by a procedure consisting of differential centrifugation, Con A-Sepharose and Blue Sepharose chromatography, PBE 94 chromatofocusing, DEAE-cellulose and gel filtration chromatography followed by preparative electrophoresis. A molecular mass of 132000 was estimated by gradient PAGE. Particular proteins were detected by Immunoelectrophoresis. Isoelectric focusing combined with Immunoelectrophoresis gave two peaks of arylsulfatase A» with isoelectric points of pH 3.9 and 4.5. Microheterogeneity of rat liver arylsulfatase A was studied by affinity immunoelectrophoresis with 9 different lectins. The presence of concanavalin A-, Lens cutinaris ag­glutinin-, Lotus tetragonolobus agglutinin- and wheat germ aggtutinin- reactive forms permitted assessment of the types of carbohydrate moieties in arylsulfatase A.

Słowa kluczowe

EN

microheterogeneity; arylosulphatase A; enzyme; purification; liver; rat; affinity immunoelectrophoresis

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 1992
• Tom: 39
• Numer: 4
• Opis fizyczny: p.355-367,fig.

Twórcy

autor

Wojczyk B.

• Jagiellonian University, Ingardena 6, 30-060 Krakow, Poland

autor

Hoja D.

autor

Litynska A.

Bibliografia

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