Dataset Information


Affinity purification and some molecular properties of human liver alkaline phosphatase.

ABSTRACT: Alkaline phosphatase from human liver was purified to homogeneity. The purification procedure included solubilization with butanol, fractionation with acetone, and chromatography on concanavalin A-Sepharose, DEAE-cellulose, Sephadex G-200 and DEAE-Sephadex. Purity was established by standard and sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. The isoelectric point of the protein was determined to be 4.0. Sephadex-gel filtration gave a mol.wt. of 146000, although a higher value was obtained in the presence of 100mM-NaC1. The subunit mol.wt. 76700, was determined by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. Neuraminidase treatment resulted in two enzyme-activity bands on isoelectric-focused gels with isoelectric points of 6.6 and 6.8. The desialylated enzyme gave only one protein band on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis with a subunit molecular weight indistinguishable from that of the non-neuraminidase-treated protein. The desialylated enzyme was more readily denatured by sodium dodecyl sulphate in the presence of mercaptoethanol than was the native enzyme.

SUBMITTER: Trepanier JM 

PROVIDER: S-EPMC1172889 | BioStudies | 1976-01-01

SECONDARY ACCESSION(S): 10.1042/bj1550653

REPOSITORIES: biostudies

Similar Datasets

1978-01-01 | S-EPMC1185841 | BioStudies
1976-01-01 | S-EPMC1163867 | BioStudies
1976-01-01 | S-EPMC1172584 | BioStudies
1981-01-01 | S-EPMC1163052 | BioStudies
1977-01-01 | S-EPMC1183715 | BioStudies
1978-01-01 | S-EPMC1183831 | BioStudies
1981-01-01 | S-EPMC1163176 | BioStudies
1985-01-01 | S-EPMC1144687 | BioStudies
1983-01-01 | S-EPMC1152145 | BioStudies
1980-01-01 | S-EPMC1161285 | BioStudies