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Substructure of human erythrocyte spectrin
Year:
1979
Authors :
Eshdat, Yuval
;
.
Volume :
10
Co-Authors:
Hsu, C.J., Dept. Pathol., Yale Univ. Sch. Med., New Haven, Conn. 06510, United States
Lemay, A., Dept. Pathol., Yale Univ. Sch. Med., New Haven, Conn. 06510, United States
Eshdat, Y., Dept. Pathol., Yale Univ. Sch. Med., New Haven, Conn. 06510, United States
Marchesi, V.T., Dept. Pathol., Yale Univ. Sch. Med., New Haven, Conn. 06510, United States
Facilitators :
From page:
227
To page:
239
(
Total pages:
13
)
Abstract:
The human erythrocyte structural protein spectrin and its subunits I and II were isolated in the presence of Na-dodecyl-sulfate by gel filtration and preparative gel electrophoresis. After removal of the detergent, spectrin alpha-helical content is comparable to spectrin isolated without detergent. Subunits I and II formed single bands in isoelectric focusing (pI = 5.6) and in Ornstein-Davis disc gel electrophoresis systems, indicating the individual subunits are homogenous in nature. The molecular weights of the subunits I and II, determined by Ferguson plot, are 237,500 land 238,600 respectively, which is in good agreement with values obtained by the standard SDS gel relative mobility method. Limited tryptic digestion of spectrin and two-dimensional peptide maps of the individual subunits cleaved by S-cyanylation reaction showed dissimilar patterns, suggesting differences in primary structure between the two subunits.
Note:
Related Files :
Amino Acids
erythrocyte membrane
human
Macromolecular Systems
Membrane Proteins
Peptide Fragments
spectrin
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Related Content
More details
DOI :
Article number:
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
27733
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:33
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Scientific Publication
Substructure of human erythrocyte spectrin
10
Hsu, C.J., Dept. Pathol., Yale Univ. Sch. Med., New Haven, Conn. 06510, United States
Lemay, A., Dept. Pathol., Yale Univ. Sch. Med., New Haven, Conn. 06510, United States
Eshdat, Y., Dept. Pathol., Yale Univ. Sch. Med., New Haven, Conn. 06510, United States
Marchesi, V.T., Dept. Pathol., Yale Univ. Sch. Med., New Haven, Conn. 06510, United States
Substructure of human erythrocyte spectrin
The human erythrocyte structural protein spectrin and its subunits I and II were isolated in the presence of Na-dodecyl-sulfate by gel filtration and preparative gel electrophoresis. After removal of the detergent, spectrin alpha-helical content is comparable to spectrin isolated without detergent. Subunits I and II formed single bands in isoelectric focusing (pI = 5.6) and in Ornstein-Davis disc gel electrophoresis systems, indicating the individual subunits are homogenous in nature. The molecular weights of the subunits I and II, determined by Ferguson plot, are 237,500 land 238,600 respectively, which is in good agreement with values obtained by the standard SDS gel relative mobility method. Limited tryptic digestion of spectrin and two-dimensional peptide maps of the individual subunits cleaved by S-cyanylation reaction showed dissimilar patterns, suggesting differences in primary structure between the two subunits.
Scientific Publication
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