Abstract
The functional properties of human hemoglobin and of isolated α- and β-chains with free SH groups blocked by 2-chloromercuri-4-nitrophenol, 4-chloromercuri-2-nitrophenol and p-chloromercuribenzoate have been determined. The oxygen affinity of all the hemoglobin derivatives is slightly higher than that of the untreated protein; the shape of the oxygen equilibrium curve is pH dependent (except for p-chloromercuribenzoate reacted hemoglobin)
Lingua originale | English |
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pagine (da-a) | 327-327-\& |
Rivista | European Journal of Biochemistry |
Volume | 22 |
DOI | |
Stato di pubblicazione | Pubblicato - 1971 |
Pubblicato esternamente | Sì |
Keywords
- HAEMOGLOBIN
- HEMOGLOBIN