Studies on Human Myoglobin
نویسندگان
چکیده
منابع مشابه
Studies on human myoglobin. II. Fetal myoglobin: its identification and its replacement by adult myoglobin during infancy.
By KARL SINGER, BASIL ANGELOPOULOS AND BRACHA RAMOT I T IS N(.)W well established that the erythrocytes of normal newborns contain about 50 to 90 per cent of fetal (type F) hemoglobin, the remainder being supplied by the normal adult (type A) pigment. As a rule, the fetal hemoglobin is rapidly replaced by the adult compound and after 7 to 12 months the embryonic pigment is no longer demonstrabl...
متن کاملStudies on Myoglobin I. the Solwility of Myoglobin in Concentrated Ammonium Sulfate Solutions
The crystallization by Theorell (8) of one of the hemoglobins of muscle, horse heart myoglobin, has made possible the more accurate study of this interesting protein, and opened the way for the investigation of other members of the series. Previously the question of the existence of a protein in the muscle resembling, but nevertheless distinct from, blood hemoglobin was in doubt. Theorell’s wor...
متن کاملStudies on the oxygen and carbon monoxide equilibria of human myoglobin.
The reactions of hemoglobin (Hb) and myoglobin (Mb) with gas are, for the particular mechanisms involved, one of the most interesting problems in biochemistry. In spite of a great number of researches on the gaseous equilibria of Hb from different animal species, Mb has not been extensively investigated from this point of view. The classical work by Theorell (1) with crystallized horse Mb appea...
متن کاملThe characterization of adult human myoglobin.
It has been reported that crystalline human myoglobin can be resolved by electrophoresis on paper into three components (1,2). Two of these possess nearly identical absorption spectra between 500 and 600 rnp and give the same reactions with oxygen. Although it was suggested that these components differ structurally (2), no evidence has been presented to support this view. In the present study t...
متن کاملProtein relaxation dynamics in human myoglobin
Transient absorption spectra in the Soret region have been measured following the photolysis of human MbCO in 75%(w/w) glycerokwater at 250,270, and 290 K. The peak of the transient difference spectrum near 436 nm shifts from low to high energy on the nanosecond time scale. The spectral changes are quantitatively analyzed using an approach based on singular value decomposition, and the results ...
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ژورنال
عنوان ژورنال: Blood
سال: 1955
ISSN: 0006-4971,1528-0020
DOI: 10.1182/blood.v10.10.979.979