Myeloperoxidase VIII: Separation into ten components by free-flow electrophoresis

Schultz, Julius; Felberg, Norman T.; John, Sosamma

doi:10.1016/0006-291x(67)90348-8

Cited by 19 publications

(2 citation statements)

References 6 publications

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“…Other more complex proteins include myeloperoxidase VIII of neutrophilis (33) with possibly 10 different subunits, deoxyribonucleic aciddependent ribonucleic acid polymerase with 4 different subunits (39), and phenol oxidase of Drosophilia melanogaster with at least 5 proteins necessary for activity (24). The characteristics of P-V are not inconsistent with a subunit structure, and the successful purification reported here now allows testing of the subunit theory.…”

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confidence: 70%

Purification and Characterization of Acid Phosphatase V from Aspergillus nidulans

Harsanyi

Dorn

1972

J Bacteriol

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Acid phosphatase V of Aspergillus nidulans was purified by ammonium sulfate precipitation, gel filtration, and ion-exchange chromatography. The enzyme demonstrated a charge microheterogeneity on starch and acrylamide gel electrophoresis, but proved to be homogeneous on ultracentrifugation and gel filtration. Phosphatase V was found to be a classic acid orthophosphoric monoester phosphohydrolase, and it cleaved p-nitrophenylphosphate, glucose-6phosphate, and uridine-5'-monophosphate at maximal rates. It was inhibited by fluoride, borate, and molybdate ions, and demonstrated end-product inhibition by inorganic phosphate. Metallic ions or cofactors were not required for activity. The molecular weight was estimated to be 100,000, the S20,w was calculated to be 4.1, and the pH optimum was found to be 6.1. Acid phosphomonoesterases (EC 3.1.3.2) are generally found in multiple molecular forms (37), and their physicochemical properties show wide variation. Within any one organism, the pH optima of the different forms may differ by several pH units (30), and the molecular weights may vary more than sixfold (6). The functional and structural relations of the various forms are often obscure and can be elucidated only by comparing the purified isozymes.

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confidence: 70%

Purification and Characterization of Acid Phosphatase V from Aspergillus nidulans

Harsanyi

Dorn

1972

J Bacteriol

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“…A technique for detecting cytochrome oxidase is useful in investigating mutations of Drosophila (1244)• Human malignant melanomas contain three forms of tyrosinase (219). Myeloperoxidase has been separated into ten components by disk (416) and free-flow (1148) electrophoresis. A method for locating red cell NADHand NADPHdiaphorases following starch-gel electrophoresis has been described (654)• Serum from patients with viral hepatitis contains two glutamic-oxalacetic transaminases, one from cytoplasm and one from mitochondria; in myocardial infarction, only the cytoplasmic form is found (32).…”

Section: Microorganismsmentioning

confidence: 99%