EurekaMag.com logo
+ Site Statistics
References:
52,725,316
Abstracts:
28,411,598
+ Search Articles
+ Subscribe to Site Feeds
EurekaMag Most Shared ContentMost Shared
EurekaMag PDF Full Text ContentPDF Full Text
+ PDF Full Text
Request PDF Full TextRequest PDF Full Text
+ Follow Us
Follow on FacebookFollow on Facebook
Follow on TwitterFollow on Twitter
Follow on Google+Follow on Google+
Follow on LinkedInFollow on LinkedIn

+ Translate

Spectrin current understanding of its physical biochemical and functional properties


Life Sciences 19(1): 1-18
Spectrin current understanding of its physical biochemical and functional properties
Spectrin consists of a complex of 2 peptides (bands 1 and 2) which have MW of about 240,000 and 220,000 daltons (.+-. 10% or more). Aggregation states of dimer, tetramer and high polymer appear to be favored. Each of the 2 bands contains multiple isoelectric, antigenic and N-terminal components; it is not known if this phenomenon is due to natural multiplicity, to proteolysis, or to the presence of non-SDS[sodium dodecyl sulfate]-dissociable subunits. Compared to myosin, the spectrin dimer is probably somewhat less .alpha.-helical and somewhat more globular. Spectrin has a weak ATPase activity which shows distinguishable Mg-ATPase and Ca-ATPase components, and band 2 of spectrin is phosphorylated by ATP-.gamma.-32P under physiologic conditions. Spectrin is present in vivo as a complex with erythrocytic actin, and after isolation will form complexes with muscle actin. The nature of these complexes is still uncertain. Spectrin interacts both with lipid bilayers (devoid of intrinsic proteins) and with the intrinsic proteins of the erythrocyte and binds Ca and ATP under appropriate conditions. These properties make it likely that spectrin controls the membrane deformability of erythrocyte (via unknown regulatory mechanisms) and is an essential component of the erythrocyte membrane in terms of its stability as an extended, flat and elastic surface. There is fragmentary evidence suggesting spectrin-like proteins exist in membranes from other cell types and possibly in cytoplasm.

Accession: 006459997

PMID: 133279

DOI: 10.1016/0024-3205(76)90368-4

Download PDF Full Text: Spectrin current understanding of its physical biochemical and functional properties



Related references

Biochemical and biophysical properties of plant storage proteins: a current understanding with emphasis on 11S seed globulins. Food Research International 32(2): 79-92, 1999

Effects of physical training on rat and guinea pig cardiac functional and biochemical properties. Federation Proceedings 39(3): ABSTRACT 141, 1980

Effects of physical training and thyroxine on rodent cardiac functional and biochemical properties. Pfluegers Archiv European Journal of Physiology 391(3): 190-194, 1981

Purification of 2 spectrin binding proteins biochemical and electron microscopic evidence for site specific reassociation between spectrin and bands 2.1 and 4.1. Proceedings of the National Academy of Sciences of the United States of America 76(10): 5192-5196, 1979

Purification of two spectrin-binding proteins: biochemical and electron microscopic evidence for site-specific reassociation between spectrin and bands 2.1 and 4.1. Proceedings of the National Academy of Sciences of the United States of America 76(10): 5192-5196, 1979

Biochemical properties of purified human erythrocyte spectrin alpha and beta chains. Journal Of Cell Biologypart 2: 284a, 1983

Biochemical and functional characterisation of casein and whey protein hydrolysates. A study on the correlations between biochemical and functional properties using multivariate data analysis. Biochemical and functional characterisation of casein and whey protein hydrolysates A study on the correlations between biochemical and functional properties using multivariate data analysis: ix + 155 pp., 2002

The alteration of the functional properties of human haemoglobin by spectrin. Experientia 33(11): 1429-1450, 1977

Physical properties of monomeric and dimeric spectrin and alpha-actinin recombinant peptides. Molecular Biology of the Cell 6(SUPPL ): 270A, 1995

The alteration of the functional properties of human hemo globin by spectrin. Experientia (Basel) 33(11): 1429-1430, 1977