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biological source
bovine eye (lens)
form
solid
impurities
Salt, essentially free
storage temp.
−20°C
Gene Information
bovine ... CRYGB(281720) , CRYGC(281722) , CRYGD(281723)
Biochem/physiol Actions
γ-Crystallin is a natural substrate for the small heat-shock protein and molecular chaperone α-crystallin. γ-Crystallin competes with Cu2+ and Zn2+ for binding to α-crystallin, reducing the latter′s chaperone capacity.
Preparation Note
Further purified from the BO-5 fraction of Chiou, S., et al., to remove βs-crystallin.
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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L R Croft
The Biochemical journal, 128(4), 961-970 (1972-07-01)
The amino acid sequence of gamma-crystallin (fraction II) from calf lens has been determined; this indicates it to be a single-chain polypeptide of 165 amino acid residues.
S H Chiou et al.
International journal of peptide and protein research, 13(4), 409-417 (1979-04-01)
The soluble proteins from bovine lens homogenate were separated on Sepharose CL-6B (2 X 200 cm) in 0.05 M tris-NaHSO3 pH 8.2 buffer containing 20 mM EDTA. Five sharp and defined fractions (HM alpha, alpha, beta H, beta L, gamma)
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