+ Translate

The primary structure of genetic variants of mouse hemoglobin

, : The primary structure of genetic variants of mouse hemoglobin. Biochemical Genetics 20(1-2): 199-208

The primary structures of the alpha globins from CE/J, DBA/2J, and a stock of Potter's mice were determined to identify the amino acid substitutions associated with the unique isoelectric focusing patterns of these hemoglobins. In addition, the primary structures of the alpha globins from MOL III and PERU mice were studied in search of amino acid substitutions that may not be detected by isoelectric focusing. CE/J hemoglobin contains a unique kind of alpha globin called chain 5. It differs from the single kind of alpha globin (chain 1) in C57BL/6 by having alanine rather than glycine at position 78. DBA/2J hemoglobin has two kinds of alpha globins: one half is like chain 5 and the other half is like chain 1. The hemoglobin from Potter's stock of Mus musculus molossinus also contains chains 1 and 5, but they are expressed at different levels i.e., 80% chain 1 and 20% chain 5. MOL III hemoglobin has a single kind of a alpha globin identical to that in C57BL/6, and PERU hemoglobin contains approximately 40% chain 1 and 60% chain 4. Chains 1 and 4 have different amino acids at positions 25, 62 and 68. These studies confirm that mouse hemoglobins separable by isoelectric focusing, but not by other means of electrophoresis, have substitutions of neutrally charged amino acids in their alpha chains.

(PDF 0-2 workdays service)

Accession: 044715687

PMID: 7092800

Submit PDF Full Text: Here

Submit PDF Full Text

No spam - Every submission is manually reviewed

Due to poor quality, we do not accept files from Researchgate

Submitted PDF Full Texts will always be free for everyone
(We only charge for PDFs that we need to acquire)

Select a PDF file:

Related references

Scaloni, A.; Pieragostini, E.; Malorni, A.; Ferrara, L.; D.L.ccia, A., 1998: Bovine hemoglobin alpha-globin chain polymorphism: primary structure determination of two new genetic variants by mass spectrometry and amino acid sequencing. The present work describes the biochemical procedures used to identify the cause of a quantitative and qualitative hemoglobin polymorphism found in Podolian cattle. First, to analyze the different phenotypes, isoelectric focusing (IEF) of hemoglob...

Chen, S.S.; Jia, P.C.; Liang, Z.Q.; Wang, L.F.; Liu, G.Y.; Huang, S.Z.; Luo, H.Y., 1981: Studies on abnormal hemoglobin variants in China. Two cases with HbG Coushatta and the primary structure of the hemoglobin variant. Chinese Medical Journal 94(1): 13-20

Lehmann, H., 1972: The primary structure of hemoglobin and its function. The hemoglobin variants. Hamatologie und Bluttransfusion 10: 359-379

Saito S., 1984: Study of abnormal hemoglobin in ehime japan 2 structural variants of hemoglobin a hemoglobin i and hemoglobin j iran and structural and synthetic variants of delta chain. During a survey for abnormal Hb in Ehime Prefecture, Shikoku, Japan, 6 cases of structural variants (1 a chain, 1 .beta. chain and 4 .delta. chain variants) and 5 cases of homozygous .delta.-thalassemia were found. From this, the frequency of visi...

Kleinschmidt, T.; Koop, B.; Braunitzer, G., 1986: The primary structure of a mouse-eared bat (Myotis velifer, Chiroptera) hemoglobin. The hemoglobin of the Mouse-Eared Bat Myotis velifer consists of one component. We present the primary structures of the alpha- and beta-globin chains which have been separated by chromatography on carboxymethyl-cellulose CM-52. The sequences have...

Garrick, M.D.; Hafner, R.; Bricker, J.; Garrick, L.M., 1974: Genetic variation in the primary structure of the beta chain of rabbit hemoglobin. Annals of the New York Academy of Sciences 241(0): 436-438

Maesiar, P.; Podhradsky, D., 1965: On Hemoglobin. Xx. Comparative Study On The Primary Structure Of Hemoglobin In Macaccus Rhesus Monkeys And Human Hemoglobin With The Use Of Combined Enzymatic Hydrolysis. Bratislavske Lekarske Listy 45: 11-20

Zimmer, T.; Bollensdorff, C.; Haufe, V.; Birch-Hirschfeld, E.; Benndorf, K., 2002: Mouse heart Na+ channels: primary structure and function of two isoforms and alternatively spliced variants. We isolated two full-length cDNA clones from the adult murine heart that encode two different voltage-gated Na+ channels: mH1 and mH2. Sequence comparisons indicated that mH1 is highly homologous to rat SCN5A, whereas mH2 is highly homologous to S...

Presnell, B.; Conti, A.; Erhardt, G.; Krause, I.; Godovac-Zimmermann, J., 1990: A rapid microbore HPLC method for determination of primary structure of beta-lactoglobulin genetic variants. A rapid method for determination of the primary structures for beta-lactoglobulin (beta-LG) genetic variants is described. This included rapid microbore HPLC, amino acid analyses, and wherever necessary, direct peptide sequencing. Two novel varian...

Ferranti, P.M.lorni, A.N.tti, G.L.ezza, P.P.zzano, R.C.ianese, L.A.deo, F., 1995: Primary structure of ovine alpha-caseins: localization of phosphorylation sites and characterization of genetic variants A, C and D. The primary structures of ovine alpha(s1)-casein variants A, C and D (formerly called Welsh variant) were determined. Separation of variants from whole casein was achieved using a fast and reliable reversed-phase HPLC method. Extended structural c...