Abstract:
:The isolation and purification of a 21,000-Da (pI 4.9) novel protein from porcine anterior pituitary and whole human pituitary is described. Comparison of the NH2-terminal sequence of the first 77 and 81 residues of the human and porcine homologs shows only one conservative substitution at residue 12, namely an Ala for a Thr between these two species. Such high sequence homology is also reflected in their amino acid composition. A computer data-bank search using a mutation data matrix and comparison with 338,327 segments of proteins revealed that this substance should be classified as belonging to a new protein superfamily. Immunocytochemical staining, using an antibody produced against a synthetic fragment, revealed the presence of immunostainable material in the anterior and posterior lobe of the pituitary and in the supraoptic nucleus of the hypothalamus. No staining was observed in the intermediate lobe of the pituitary. Furthermore, purified neurointermediate lobe secretory granule preparations were also shown to contain this novel polypeptide.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
Seidah NG,Hsi KL,De Serres G,Rochemont J,Hamelin J,Antakly T,Cantin M,Chrétien Mdoi
10.1016/0003-9861(83)90063-2subject
Has Abstractpub_date
1983-09-01 00:00:00pages
525-34issue
2eissn
0003-9861issn
1096-0384pii
0003-9861(83)90063-2journal_volume
225pub_type
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journal_title:Archives of biochemistry and biophysics
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更新日期:2015-05-15 00:00:00
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