Thermal and acid denaturation of bovine lens α-crystallin

2011 ◽  
Vol 79 (6) ◽  
pp. 1747-1758 ◽  
Author(s):  
Tue Rasmussen ◽  
Marco van de Weert ◽  
Wim Jiskoot ◽  
Marina R. Kasimova
Keyword(s):  
Acid Denaturation ◽  
Bovine Lens

scholarly journals The solubility of bovine lens crystallins.

1981 ◽  
Vol 256 (13) ◽  
pp. 6523-6525
Author(s):  
E.Q. Lawson ◽  
C.F. Schubert ◽  
R.V. Lewis ◽  
C.R. Middaugh
Keyword(s):  
Lens Crystallins ◽  
Bovine Lens

scholarly journals Sequence analysis of bovine lens aldose reductase.

1990 ◽  
Vol 265 (7) ◽  
pp. 3628-3635
Author(s):  
S Z Schade ◽  
S L Early ◽  
T R Williams ◽  
F J Kézdy ◽  
R L Heinrikson ◽  
...  
Keyword(s):  
Sequence Analysis ◽  
Aldose Reductase ◽  
Bovine Lens

scholarly journals The nucleotide sequence of two bovine lens phenylalanine tRNAs. Possible activation of a new phenylalanine tRNA gene during differentiation of lens cells.

1980 ◽  
Vol 255 (13) ◽  
pp. 6020-6023
Author(s):  
F.K. Lin ◽  
T.D. Furr ◽  
S.H. Chang ◽  
J. Horwitz ◽  
P.F. Agris ◽  
...  
Keyword(s):  
Nucleotide Sequence ◽  
Trna Gene ◽  
Bovine Lens ◽  
Lens Cells

scholarly journals Evaluation of non-thermal microwave effects on bovine lens by measuring S-parameters induced by variations in dielectric coefficient

IEEE Access ◽  
2021 ◽  
pp. 1-1
Author(s):  
Junqing Lan ◽  
Xiaofeng Sun ◽  
Huacheng Zhu ◽  
Xiaoren Cao ◽  
Lan Yang ◽  
...  
Keyword(s):  
Bovine Lens ◽  
S Parameters ◽  
Dielectric Coefficient ◽  
Microwave Effects

scholarly journals Reaction of tyrosine oxidation products with proteins of the lens

1968 ◽  
Vol 109 (2) ◽  
pp. 301-305 ◽  
Author(s):  
Antoinette Pirie
Keyword(s):  
Ascorbic Acid ◽  
Fluorescence Spectra ◽  
Ferrous Sulphate ◽  
Oxidation Products ◽  
Thiol Groups ◽  
Lens Proteins ◽  
Bovine Lens ◽  
Tyrosine Oxidation ◽  
Cataractous Lens

Oxidation of tyrosine in the presence of bovine lens proteins leads to the formation of brown or black melanoproteins. Both tyrosinase and the oxidizing system of ferrous sulphate–ascorbic acid–EDTA are effective. The fluorescence of the lens proteins is both altered and enhanced by the tyrosine-oxidizing systems. Their fluorescence spectra resemble those of urea-insoluble proteins of human cataractous lens and of 1,2-naphthaquinone–proteins of naphthalene cataract. The lens proteins lose their thiol groups and, in acid hydrolysates of treated β-and γ-crystallins, a substance has been detected chromatographically that behaves similarly to a compound formed when 3,4-dihydroxyphenylalanine (dopa) is oxidized by tyrosinase in the presence of cysteine. Analysis and behaviour of this substance from hydrolysates of lens proteins suggest that it is a compound of cysteine and dopa.

Kinetic Evidence on the Mechanism of the Acid Denaturation of Horse CO Hemoglobin1

1951 ◽  
Vol 73 (12) ◽  
pp. 5568-5572 ◽  
Author(s):  
Ethel M. Zaiser ◽  
Jacinto Steinhardt
Keyword(s):  
Acid Denaturation

scholarly journals Study of the Chaperoning Mechanism of Bovine Lens α-Crystallin, a Member of the α-Small Heat Shock Superfamily

2001 ◽  
Vol 80 (4) ◽  
pp. 1986-1995 ◽  
Author(s):  
Saïd Abgar ◽  
Jos Vanhoudt ◽  
Tony Aerts ◽  
Julius Clauwaert
Keyword(s):  
Heat Shock ◽  
Bovine Lens
Sign in / Sign up

Export Citation Format

Share Document