Výsledky vyhledávání

Selective active site inhibitors of human lactate dehydrogenases A4, B4, and C4

Autor: Y, Yu, J A, Deck, L A, Hunsaker, L M, Deck, R E, Royer, E, Goldberg, D L, Vander Jagt

Publikováno v: Biochemical pharmacology. 62(1)

Human lactate dehydrogenases (LDH-A4, -B4, and -C4) are highly homologous with 84-89% sequence similarities and 69-75% amino acid identities. Active site residues are especially conserved. Gossypol, a natural product from cotton seed, is a non-select

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::cd38d3298ce72c4efaf9165d328e5711
https://pubmed.ncbi.nlm.nih.gov/11377399

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Isolation and characterization of the multiple glutathione S-transferases from human liver. Evidence for unique heme-binding sites

Autor: D L, Vander Jagt, L A, Hunsaker, K B, Garcia, R E, Royer

Publikováno v: The Journal of biological chemistry. 260(21)

Thirteen forms of glutathione S-transferase were isolated from human liver in high yields by glutathione-affinity chromatography and chromatofocusing. Apparent isoelectric points ranged from 4.9 to 8.9 and included neutral forms. All 13 forms appeare

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::d8e942caa06d3b179509d290dd25c29e
https://pubmed.ncbi.nlm.nih.gov/4044571

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