Spectrin bands 1 and 2 are antigenically distinct and are not composed of subunits

Journal Article · Wed Feb 01 04:00:00 EST 1978 · Arch. Biochem. Biophys.; (United States)

DOI:https://doi.org/10.1016/0003-9861(78)90456-3· OSTI ID:6425800

Kirkpatrick, F H; Rose, D J; La Celle, P

Human erythrocyte membranes and freshly isolated spectrin were separated into their constituent peptides by sodium dodecyl sulfate--polyacrylamide gel electrophoresis. The peptides were electrophoresed from slices of such gels into agarose gels containing anti-spectrin antibodies and Triton X-100. In fresh preparations, precipitin arcs were observed only against peptides migrating as bands 1 and 2. It was found that bands 1 and 2 did not cross-react. There were two major arcs from band 1 and one principal arc from band 2, plus minor splitting of these arcs. None of the band 1 arc fused with band 2 arc. In fresh erythrocyte ghosts only bands 1 and 2 reacted with anti-spectrin; bands 2.1, 3, and 5, in particular, showed no precipitin arcs. However, in aged ghosts, arc appeared in the band 3 region; in aged isolated spectrin, arcs appeared in the band 2.1 region; and in trypsin-degraded spectrin, reactive species occurred in all molecular weight classes. It is concluded that spectrin has no subunits smaller than 220,000 molecular weight and that bands 1 and 2 are immunochemically distinct.

• Research Organization: Univ. of Rochester, NY
• OSTI ID: 6425800
• Journal Information: Arch. Biochem. Biophys.; (United States), Journal Name: Arch. Biochem. Biophys.; (United States) Vol. 186:1; ISSN ABBIA
• Country of Publication: United States
• Language: English

Related Subjects

550300* -- Cytology
59 BASIC BIOLOGICAL SCIENCES
ANIMALS
BIOLOGICAL MATERIALS
BLOOD
BLOOD CELLS
BODY FLUIDS
ELECTROPHORESIS
ERYTHROCYTES
MAMMALS
MAN
MOLECULAR WEIGHT
ORGANIC COMPOUNDS
PEPTIDES
POLYPEPTIDES
PRIMATES
PROTEINS
VERTEBRATES