l homoarginine/рак

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Effect of hyperosmolality on alkaline phosphatase and stress-response protein 27 of MCF-7 breast cancer cells.

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MCF-7, a continuous cell line derived from a human breast carcinoma, exhibits very low alkaline phosphatase (ALP) activity. The enzyme is heat-stable and is inhibited by L-phenylalanine and L-phenylalanylglycylglycine, but not by L-homoarginine, 1-bromotetramisole, or levamisole. These data indicate

Electrophoretic patterns of alkaline phosphatase isoenzymes in human sera with abnormally high activity, and an unusual band observed in sera of patients with pancreatic cancer.

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Alkaline phosphatase isoenzymes in sera were resolved by electrophoresis on cellulose acetate membranes into seven different bands (L1, B, Pl, L2, l1, l2, and Pa, in decreasing order of electrophoretic mobility). The slowest moving band (Pa) was observed in the sera of 16 patients--15 with cancer of

Direct immunoperoxidase staining for Regan isoenzyme of alkaline phosphatase in human tumor tissues.

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Immunoperoxidase staining for Regan isoenzyme of alkaline phosphatase was performed on cryostat sections of five human tumor tisssues. With a direct immunoperoxidase staining for the localization of Regan isoenzyme at the light and electron microscope levels, sections previously fixed with 0.05 M

Inhibitory effect of L-homoarginine on murine osteosarcoma cell proliferation.

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An organ-specific alkaline phosphatase inhibitor, L-homoarginine, at 44.5 mM concentration inhibited [3H]thymidine uptake by C3H/He mouse osteosarcoma (OS) cells, while L-arginine, L-phenylalanine, and glycine had little effect on the uptake. This inhibitory effect of L-homoarginine persisted even

[Inhibitory effect of L-homoarginine on murine osteosarcoma cell proliferation].

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An organ-specific alkaline phosphatase (AIP) inhibitor, L-homoarginine at 44.5 mM concentration inhibited 3H-thymidine uptake by mouse C3H/He osteosarcoma (OS) cells, while L-arginine, L-phenylalanine and L-glycine had little effect on the uptake. This inhibitory effect by L-homoarginine persisted

Human osteogenic sarcoma: fine structural localization of adenosine triphosphatase.

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The localization of ATPases in 7 osteogenic sarcomas of osteoblastic, chondroblastic and fibroblastic type was investigated at the fine structural level using two types of substrates: one with lead as capturing ion and one with strontium (the latter presumed to reveal sites of Na+-K+-dependent

Specific amino acid (L-arginine) requirement for the microbiostatic activity of murine macrophages.

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The microbiostatic action of macrophages was studied in vitro employing peritoneal cytotoxic macrophages (CM) from mice acting against Cryptococcus neoformans cultured in Dulbecco's medium with 10% dialyzed fetal bovine serum. Fungistasis was measured using electronic particle counting after lysis

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