EurekaMag.com logo
+ Translate

Spectrin current understanding of its physical biochemical and functional properties


, : Spectrin current understanding of its physical biochemical and functional properties. Life Sciences 19(1): 1-18

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


Submit PDF Full Text

No spam - Every submission is manually reviewed

Due to poor quality, we do not accept files from Researchgate

Submitted PDF Full Texts will always be free for everyone
(We only charge for PDFs that we need to acquire)

Select a PDF file:
Close
Close

Related references

Marcone, M.F., 1999: Biochemical and biophysical properties of plant storage proteins: a current understanding with emphasis on 11S seed globulins. The increased use of non-cereal grains as supplements for nutritional and functional foods purposes will require a more in-depth understanding of the 11S globulin (their main storage protein). Studies indicate that 11S globulins from both mono- an...

Baldwin K.M.; Ernst S.B.; Herrick R.E.; Matsuda D.K., 1980: Effects of physical training on rat and guinea pig cardiac functional and biochemical properties. Federation Proceedings 39(3): ABSTRACT 141

Baldwin K.M.; Ernst S.B.; Herrick R.E.; Macintosh A.M., 1981: Effects of physical training and thyroxine on rodent cardiac functional and biochemical properties. The effects of 8 wk of interval running and of 14 days of thyroxine treatment were studied on selected cardiac functional and biochemical parameters of contraction in female guinea pigs and rats. Relative to their respective sendentary-control gro...

Tyler, J.M.; Hargreaves, W.R.; Branton, D., 1979: Purification of 2 spectrin binding proteins biochemical and electron microscopic evidence for site specific reassociation between spectrin and bands 2.1 and 4.1. Two peripheral proteins of the human erythrocyte membrane that are capable of forming a stable complex with spectrin were purified. The proteins, band 2.1 (MW 210,000) and band 4.1 (MW 82,000), are water soluble and exist as monomers in solution....

Tyler, J.M.; Hargreaves, W.R.; Branton, D., 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. Two peripheral proteins of the human erythrocyte membrane that are capable of forming a stable complex with spectrin have been purified. The proteins, band 2.1 (Mr 210,000) and band 4.1 (Mr 82,000), are water soluble and exist as monomers in solut...

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

Ven, C. van der, 2002: Biochemical and functional characterisation of casein and whey protein hydrolysates. A study on the correlations between biochemical and functional properties using multivariate data analysis. Whey protein concentrate and sodium caseinate were hydrolysed with commercially available enzyme preparations. The resulting hydrolysates were characterized using several analytical characterization methods and by determination of several function...

Devogel, M.; Léonis, J.; Vincentelli, J., 1977: The alteration of the functional properties of human haemoglobin by spectrin. Kinetic investigation by means of stopped flow techniques showed the rate of deoxygenation of haemoglobin to be slower in the presence of spectrin. At pH 7.15, the kinetic constant was 27.2 sec-1 in presence of spectrin instead of 34.3 sec-1 for h...

Best, S.L.; Desilva, T.M.; Ursitti, J.A.; Speicher, D.W., 1995: Physical properties of monomeric and dimeric spectrin and alpha-actinin recombinant peptides. Molecular Biology of the Cell 6(SUPPL ): 270A

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