Cyanate formation in solutions of urea II. Effect of urea on the eye lens protein α-crystallin
TLDR
It has been demonstrated by comparative electrophoresis on polyacryalmide gels, that long contact of α-crystallin with urea eventually gives rise to a high degree of carbamylation which may lead to erroneous conclusions about the number of real subunits.About:
This article is published in Biochimica et Biophysica Acta.The article was published on 1971-09-28 and is currently open access. It has received 57 citations till now. The article focuses on the topics: Urea.read more
Citations
More filters
Journal ArticleDOI
Structural proteins of the mammalian lens: a review with emphasis on changes in development, aging and cataract.
John J. Harding,Keith J. Dilley +1 more
Journal ArticleDOI
On the Subunit Structure of the Protein of Human Serum High Density Lipoprotein I. A STUDY OF ITS MAJOR POLYPEPTIDE COMPONENT (SEPHADEX, FRACTION III)
TL;DR: The results of the present studies were taken to indicate that HDL2 contains at least two polymorphic forms of III having equimolecular weight, but differing slightly in chemical composition and associated together by noncovalent linkage.
Journal ArticleDOI
Fractionation of the C-apoproteins from human plasma very low density lipoproteins.
TL;DR: It is demonstrated that the use of urea at room temperature can lead to the production of artifactual polymorphism through carbamylation of the C-apolipoproteins.
References
More filters
Journal ArticleDOI
The use of cyanate for the determination of NH2-terminal residues in proteins.
George R. Stark,Derek G. Smyth +1 more
Journal ArticleDOI
Cyanate formation in solutions of urea. I. Calculation of cyanate concentrations at different temperature and pH.
TL;DR: Data from the literature on the equilibrium between urea and cyanate which were difficult to combine, have been correlated by computer calculation and accumulation of cyanate in urea solutions was quantitatively studied.
Journal ArticleDOI
Subunits of alpha-crystallin from adult and embryonic cattle lens.
TL;DR: The electrophoresis patterns of α-crystallin on polyacrylamide gel containing 6 M urea at alkaline pH suggest a considerable heterogeneity of the subunits, but only two bands can be observed either at acid pH or in 1 per cent sodium dodecylsulphate at alkalin pH8.
Journal ArticleDOI
Investigations on the polypeptide chains of α-crystallin
TL;DR: From analyses of the fragments produced after cyanogen bromide cleavage it can be concluded that at least two different types of subunits are present in the α-crystallin aggregate.
Journal ArticleDOI
Report on the symposium on the biochemistry of the lens
TL;DR: The Symposium was devoted primarily to the biochemistry of the proteins of the lens, and the chemical and physiological structure, the immunological reactions of the water soluble and water insoluble lens proteins was discussed.
Related Papers (5)
Reactions of the Cyanate Present in Aqueous Urea with Amino Acids and Proteins
The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis
Klaus Weber,Mary Osborn +1 more