Abstract:
:alpha and beta chains from adult hemoglobin of the slender loris (Loris tardigradus) were isolated by Amberlite CG-50 column chromatography. After S-aminoethylation, both chains were digested with trypsin and the amino acid sequences of the tryptic peptides obtained were analyzed. Further, the order of these tryptic peptides in each chain was deduced from their homology with the primary structures of alpha and beta chains of human adult hemoglobin. Comparing the primary structures of the alpha and beta chains of adult hemoglobin of the slender loris thus obtained with those of adult hemoglobin of the slow loris, 4 amino acid substitutions in the alpha chains and 2 in the beta chains were recognized.
journal_name
J Biochemjournal_title
Journal of biochemistryauthors
Maita T,Goodman M,Matsuda Gdoi
10.1093/oxfordjournals.jbchem.a132138keywords:
subject
Has Abstractpub_date
1978-08-01 00:00:00pages
377-83issue
2eissn
0021-924Xissn
1756-2651journal_volume
84pub_type
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