PMID: 7011415Feb 27, 1981Paper

The secondary structure of ovomucoid and its domains as studied by circular dichroism

Biochimica Et Biophysica Acta
K WatanabeY Sato

Abstract

The secondary structure of chicken egg white ovomucoid and its domains was studied by means of circular dichroism (CD). The various domains (domain I, domains II . III, domains I . II, and domain III with and without carbohydrate) were prepared from the ovomucoid by cyanogen bromide cleavage and Staphylococcus aureus protease V-8 digestions. The carbohydrate moiety in the ovomucoid was isolated after its extensive pronase and endo-beta-N-acetyl-glucosaminidase H digestions. On the net CD spectra of polypeptide chain in the ovomucoid and domain preparations, which were obtained by subtracting the spectrum of the carbohydrate moiety from their spectra, the fractions of secondary structure were calculated by the method of Chang et al. (Chang, C.T., Wu, C.S.C. and Yang, J.T. (1978) Anal. Biochem. 91, 13-31). The estimated composition of the secondary structure in the ovomucoid was as follows: alpha-helix, 26%; beta-structure, 46%; beta-turn, 10%; and random coil, 18%. The secondary structure compositions estimated for the three domains suggested that domains I and II were homologous to one another but not to domain III in regard to the proportion of secondary structure content.

References

May 1, 1976·The Biochemical Journal·J G Beeley
Apr 1, 1975·The Biochemical Journal·A Waheed, A Salhuddin
Jan 26, 1972·Biochimica Et Biophysica Acta·T Takagi, N Ito
Feb 26, 1968·Biochemical and Biophysical Research Communications·I Listowsky, S Englard
Apr 1, 1968·Journal of Biochemistry·K IkedaT Ikenaka
Dec 28, 1966·Biochimica Et Biophysica Acta·M M SimlotR E Feeney
Nov 1, 1978·Analytical Biochemistry·C T ChangJ T Yang
Dec 28, 1964·Annals of the New York Academy of Sciences·B J DAVIS

❮ Previous
Next ❯

Citations

Dec 1, 1993·Protein Science : a Publication of the Protein Society·L Swint, A D Robertson
May 22, 2004·European Journal of Biochemistry·Leopoldo G GebhardMario R Ermácora
Oct 16, 2007·Protein Expression and Purification·Klaus VitzithumUte C Marx
May 10, 2013·Analytical and Bioanalytical Chemistry·Alla SynytsyaVladimír Setnička
Dec 7, 2017·Journal of the Science of Food and Agriculture·Nicoleta StănciucIuliana Aprodu
Jun 29, 1981·Biochimica Et Biophysica Acta·T MatsudaY Sato
Apr 27, 1984·Biochimica Et Biophysica Acta·K NittaK E Ebner
Sep 22, 1982·Biochimica Et Biophysica Acta·T MatsudaR Nakamura
May 25, 2021·Biochemistry and Biophysics Reports·Laritza RojasYamile González-González
Jun 14, 1985·Biochemical and Biophysical Research Communications·T MatsudaK Shimokata
Oct 21, 1986·Biochemistry·K Gekko, Y Hasegawa
Oct 18, 2013·The Journal of Physical Chemistry. B·Asaf Grupi, Allen P Minton

❮ Previous
Next ❯

Related Concepts

Related Feeds

Cajal Bodies & Gems

Cajal bodies or coiled bodies are dense foci of coilin protein. Gemini of Cajal bodies, or gems, are microscopically similar to Cajal bodies. It is believed that Cajal bodies play important roles in RNA processing while gems assist the Cajal bodies. Find the latest research on Cajal bodies and gems here.