The Amino Acid Composition of Some Mammalian Hemoglobins: Mouse, Guinea Pig, and Elephant.
نویسنده
چکیده
Previous work (1, 2) suggested that a relationship might exist between the number of reactive cysteine residues in various mammalian hemoglobins and the body weight of the animal from which the hemoglobin comes. These studies depended on amperometric titration of the deoxygenated hemoglobin with mercuric ions. The number of mercuric ions bound per molecule ranged from 1.29 for elephant hemoglobin to 3.66 for mouse hemoglobin. This was interpreted as a variation in the number of “available” -SH groups. However, the amperometric titration procedure suffers from the difficulty in identifying unequivocally the groups involved. The present studies were undertaken primarily to determine whether the cysteine content (as distinct from “availability”) of chromatographically purified mouse hemoglobin of a specific strain differs significantly from that of the hemoglobins of larger mammals.
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عنوان ژورنال:
- The Journal of biological chemistry
دوره 238 شماره
صفحات -
تاریخ انتشار 1963