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A Koelliker hemoglobin in chick erythrocytes.
- Source :
-
Comparative biochemistry and physiology. B, Comparative biochemistry [Comp Biochem Physiol B] 1987; Vol. 87 (4), pp. 1025-32. - Publication Year :
- 1987
-
Abstract
- 1. Adult chicken hemoglobins were analysed by ion exchange chromatography and isoelectric focusing and a minor hemoglobin fraction (HbK) was isolated. 2. Analysis of the constituent chains shows that HbK differs from the two major hemoglobins HbA and HbD in the alpha globin. 3. The amino acid composition, the tryptic peptide maps, the results of carboxypeptidase digestion and the functional properties show that the HbK alpha globin is quite similar to that of HbA except that the C-terminal amino acid Arg 141 is lacking. 4. HbK must then be considered a Koelliker-type hemoglobin.
- Subjects :
- Amino Acids analysis
Animals
Carboxypeptidases
Carboxypeptidases A
Hemoglobin A isolation & purification
Hemoglobins, Abnormal metabolism
Macromolecular Substances
Oxyhemoglobins metabolism
Peptide Mapping
Trypsin
Chickens blood
Erythrocytes analysis
Hemoglobins, Abnormal isolation & purification
Subjects
Details
- Language :
- English
- ISSN :
- 0305-0491
- Volume :
- 87
- Issue :
- 4
- Database :
- MEDLINE
- Journal :
- Comparative biochemistry and physiology. B, Comparative biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 3665417
- Full Text :
- https://doi.org/10.1016/0305-0491(87)90428-7