Much recent work has dealt with water-soluble analogs of the naturally occurring porphyrins as a means of gaining a more detailed understanding of the in viva functioning of such metal macrocyclic complexes [l-9]. Interest in metalloporphyrin-protein complexes arises from the crucial role these spec
Reactions of water-soluble metalloporphyrins with the serum protein, hemopexin
β Scribed by Gibbs, Esther; Skowronek, William R.; Morgan, William T.; Muller-Eberhard, U.; Pasternack, Robert F.
- Book ID
- 126812530
- Publisher
- American Chemical Society
- Year
- 1980
- Tongue
- English
- Weight
- 661 KB
- Volume
- 102
- Category
- Article
- ISSN
- 0002-7863
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The substitution reections of tetrekis+l-N-methylpyridyl)porphinecobdt (III) (CoHITMpyP) with aside and with 1 .1.3.3-tetrametltyl-2-thiourea (TMTU) have been studied as a function of pH at 25" and en ionic strength of 0.5 M. The mechanistic pathway proposed for thiocyanate [l] and pyridine [2] is a
Complex formation between polyacrylic acid (PAA) and bovine serum albumin (BSA), human serum albumin (HSA), hemoglobin (Hb), globin (GI), and, respectively, transferrin (Tr), were studied in neutral water. Water-soluble and insoluble complexes are formed upon addition of divalent copper ions to the