The Amino Acid Sequence of -crystallin (fraction II) from Calf Lens

Overview

Journal Biochem J

Specialty Biochemistry

Date 1972 Jul 1

PMID 4674126

Citations 21

Authors

L R Croft

Affiliations

Soon will be listed here.

Abstract

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.

Citing Articles

Primary sequence contribution to the optical function of the eye lens.

Mahendiran K, Elie C, Nebel J, Ryan A, Pierscionek B Sci Rep. 2014; 4:5195.

PMID: 24903231 PMC: 4047532. DOI: 10.1038/srep05195.

Intermolecular protein interactions in solutions of bovine lens beta L-crystallin. Results from 1/T1 nuclear magnetic relaxation dispersion profiles.

Koenig S, Brown 3rd R, Kenworthy A, Magid A, Ugolini R Biophys J. 1993; 64(4):1178-86.

PMID: 8388267 PMC: 1262435. DOI: 10.1016/S0006-3495(93)81483-8.

Multiple gamma-crystallins of the mouse lens: fractionation of mRNAs by cDNA cloning.

Shinohara T, Robinson E, Appella E, Piatigorsky J Proc Natl Acad Sci U S A. 1982; 79(9):2783-7.

PMID: 6953430 PMC: 346290. DOI: 10.1073/pnas.79.9.2783.

Biochemical evidence for membrane disintegration in human cataracts.

Garner M, Roy D, Rosenfeld L, Garner W, Spector A Proc Natl Acad Sci U S A. 1981; 78(3):1892-5.

PMID: 6785760 PMC: 319241. DOI: 10.1073/pnas.78.3.1892.

The prediction of repetitive protein sequences from amino acid compositions.

Harding J Biochem J. 1984; 217(1):339-40.

PMID: 6696728 PMC: 1153218. DOI: 10.1042/bj2170339.

References

Carnegie P . Digestion of an arg-pro bond by trypsin in the ecephalitogenic basic protein of human myelin. Nature. 1969; 223(5209):958-9. DOI: 10.1038/223958a0. View

Croft L, WALEY S . Structural studies on bovine -crystallin. Biochem J. 1971; 121(3):453-9. PMC: 1176593. DOI: 10.1042/bj1210453. View

WALEY S, Watson J . The action of trypsin on polylysine. Biochem J. 1953; 55(2):328-37. PMC: 1269242. DOI: 10.1042/bj0550328. View

Testa M, Fiore C, BOCCI N, Calabro S . Effect of the oxidation of sulfhydryl groups on lens proteins. Exp Eye Res. 1968; 7(2):276-90. DOI: 10.1016/s0014-4835(68)80079-x. View

Liu T, Chang Y . Hydrolysis of proteins with p-toluenesulfonic acid. Determination of tryptophan. J Biol Chem. 1971; 246(9):2842-8. View

Heilmann J, BARROLLIER J, WATZKE E . [Amino acid determination on paper chromatograms]. Hoppe Seylers Z Physiol Chem. 1957; 309(4-6):219-20. View

Yamada S, Itano H . Phenanthrenequinone as an analytical reagent for arginine and other monosubstituted guanidines. Biochim Biophys Acta. 1966; 130(2):538-40. DOI: 10.1016/0304-4165(66)90256-x. View

Croft L . C-terminal amino acid sequence of bovine -crystallin. Biochem J. 1971; 121(3):557-9. PMC: 1176605. DOI: 10.1042/bj1210557. View

Gaitonde M, Dovey T . A rapid and direct method for the quantitative determination of tryptophan in the intact protein. Biochem J. 1970; 117(5):907-11. PMC: 1179049. DOI: 10.1042/bj1170907. View

10.

Woods K, Wang K . Separation of dansyl-amino acids by polyamide layer chromatography. Biochim Biophys Acta. 1967; 133(2):369-70. DOI: 10.1016/0005-2795(67)90078-5. View

11.

BJORK I . Studies on gamma-crystallin from calf lens. I. Isolation by gel filtration. Exp Eye Res. 1961; 1:145-54. DOI: 10.1016/s0014-4835(61)80020-1. View

12.

DeLange R, Fambrough D, Smith E, Bonner J . Calf and pea histone IV. I. Amino acid compositions and the identical COOH-terminal 19-residue sequence. J Biol Chem. 1968; 243(22):5906-13. View

13.

Offord R . Electrophoretic mobilities of peptides on paper and their use in the determination of amide groups. Nature. 1966; 211(5049):591-3. DOI: 10.1038/211591a0. View

14.

Smyth D, STEIN W, Moore S . The sequence of amino acid residues in bovine pancreatic ribonuclease: revisions and confirmations. J Biol Chem. 1963; 238:227-34. View

15.

Matsubara H, Sasaki R, Chain R . Spinach ferredoxin. I. Amino acid composition and terminal sequences. J Biol Chem. 1968; 243(8):1725-31. View

16.

Charlton J, VAN HEYNINGEN R . An investigation into the loss of proteins of low molecular size from the lens in senile cataract. Exp Eye Res. 1968; 7(1):47-55. DOI: 10.1016/s0014-4835(68)80025-9. View

17.

Zigman S . Eye lens color: formation and function. Science. 1971; 171(3973):807-9. DOI: 10.1126/science.171.3973.807. View