Feb 1, 1976

Cathepsin, phosphoprotein-phosphatase and acid phosphatase in the soluble fraction of the cattle brain cortex: purification and properties (author's transl)

Journal of Clinical Chemistry and Clinical Biochemistry. Zeitschrift Für Klinische Chemie Und Klinische Biochemie
E Albert

Abstract

Cattle brain cortex was homogenised in 0, 29 mol/1 sucrose and centrifuged at 101 000 X g. The supernatant contains the majority of 3 enzymes participating in protein turnover: cathepsin (EC 3.4.4.23), phosphoprotein phosphatase (EC 3.1.3.16) and acid phosphatase (EC 3.1.3.2). They were separated by chromatography on Sephadex G 200 in neutral buffer. The cathepsin was purified up to 380 fold by gel filtration on Sephadex and column electrophoresis. The pH optimum of cathepsin was 5.7. At 37 degrees C no decrease of activity was measurable during 30 min. The Km was found to be 2.75 mg/ml Casein Hammarsten. The molecular weight by gel filtration and exclusion-gel electrophoresis was about 45 000, corresponding to the cathepsin from human liver (Barrett, A.J. (1970) Biochem. J. 117, 601-607). The sedimentation constant 3.0 S20,W is comparable with the values of proteinase of different origin, and the composition is similar with respect to the high proportion of acidic amino acids. The phosphoprotein phosphatase can be further purified by chromatography on hydroxyapatite and by column electrophoresis. The pH optimum of phosphoprotein phosphatase was about pH 5.5. At 45 degrees C no decrease of activity was measurable during 20 min;...Continue Reading

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Mentioned in this Paper

Casein allergenic extract
Acid Phosphatase
Sephadex G 200
Cortex Bone Disorders
Adrenal Cortex Diseases
Barrett Esophagus
Caseins
Phosphoric Monoester Hydrolases
Enzymes, antithrombotic
DUSP22 protein, human

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