Instability of DTNB-treated globin or haemoglobin
| Autor: | Allan R Nash, Eop Thompson, N. G. Baptist |
|---|---|
| Rok vydání: | 1976 |
| Předmět: |
Iodoacetic acid
Chemical Phenomena DTNB Sodium Size-exclusion chromatography chemistry.chemical_element Dithionitrobenzoic Acid chemistry.chemical_compound Hemoglobins Endocrinology Polymer chemistry Genetics Humans General Materials Science Trypsin Globin Disulfides Molecular Biology Polyacrylamide gel electrophoresis chemistry.chemical_classification Carbocysteine General Medicine Electrophoresis Cellulose Acetate Chromatography Ion Exchange Peptide Fragments Globins Molecular Weight Chemistry Reproductive Medicine Biochemistry chemistry Ethylmaleimide Nitrobenzoates Urea Thiol Cystine Animal Science and Zoology Developmental Biology Biotechnology |
| Zdroj: | Australian journal of biological sciences. 29(3) |
| ISSN: | 0004-9417 |
| Popis: | Human haemoglobin or globin in its native form reacts with 5,5'-dithiobis(2-nitrobenzoic acid) (DTNB) with uptake of two 3-carboxylato-4-nitrothiophenol groups, one for each of the reactive thiols at the {393 positions. Attempts to isolate the DTNB-treated globin by the acetone-Hel method, which unfolds the protein chains, result in disulphide interchange and oxidation of almost all the uncoupled 'masked' thiol groups. This modification is in marked contrast to the stability of haemoglobin or globin treated with reagents such as iodoacetic acid or N-ethylmaleimide that do not form disulphide bonds in blocking the thiol groups. The derivatized globin chains have been separated by urea-thiol buffer chromatography on carboxymethylcellulose columns. Amino acid analysis and peptide mapping established the presence and location of disulphide bonds, whilst gel filtration in urea buffers and sodium dodecyl sulphate acrylamide gel electrophoresis defined the size of the products. |
| Databáze: | OpenAIRE |
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