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Literature DB >> 4983823

Aging of alpha-crystallins during development of the lens.

Abstract

Fetal alpha-crystallin from the bovine lens can be resolved into three major subunit fractions by ion exchange chromatography. A fourth subunit gradually arises during the development of the lens. Incorporation studies indicate that this subunit is not formed by de novo synthesis but by the chemical conversion of one subunit into another. Possible mechanisms for this conversion are discussed.

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Year: 1969 PMID： 4983823 PMCID： PMC286176 DOI： 10.1073/pnas.64.1.404

Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205

9 in total

1. DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS.

Authors: B J DAVIS
Journal: Ann N Y Acad Sci Date: 1964-12-28 Impact factor: 5.691

2. The preparation and enzymatic hydrolysis of reduced and S-carboxymethylated proteins.

Authors: A M CRESTFIELD; S MOORE; W H STEIN
Journal: J Biol Chem Date: 1963-02 Impact factor: 5.157

3. The ontogeny of chick embryo hemoglobin.

Authors: F H WILT
Journal: Proc Natl Acad Sci U S A Date: 1962-09-15 Impact factor: 11.205

4. Splitting and recombination of alpha-crystallin.

Authors: H BLOEMENDAL; W S BONT; J F JONGKIND; J H WISSE
Journal: Exp Eye Res Date: 1962-06 Impact factor: 3.467

5. Increase in the complexity of alpha-crystallins during differentiation of lens cells.

Authors: W G Palmer; J Papaconstantinou
Journal: Nature Date: 1968-07-13 Impact factor: 49.962

6. Hemoglobin synthesis during amphibian metamorphosis. I. Chemical studies on the hemoglobins from the larval and adult stages of Rana catesbeiana.

Authors: B Moss; V M Ingram
Journal: J Mol Biol Date: 1968-03-28 Impact factor: 5.469

7. The primary structure of Golfingia gouldii hemerythrin. Oder of peptides in fragments produced by tryptic digestion of succinylated hemerythrin. Complete amino acid sequence.

Authors: G L Klippenstein; J W Holleman; I M Klotz
Journal: Biochemistry Date: 1968-11 Impact factor: 3.162

8. Biochemistry of bovine lens proteins. 3. Chemical and physical properties of alpha-crystallin subunits.

Authors: W G Palmer; J Papaconstantinou
Journal: Biochemistry Date: 1968-01 Impact factor: 3.162

9. Lactate dehydrogenase isozymes and their relationship to lens cell differentiation.

Authors: J A Stewart; J Papaconstantinou
Journal: Biochim Biophys Acta Date: 1966-05-26

9 in total

8 in total

Aging of alpha-crystallins during development of the lens.

1. DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS.

2. The preparation and enzymatic hydrolysis of reduced and S-carboxymethylated proteins.

3. The ontogeny of chick embryo hemoglobin.

4. Splitting and recombination of alpha-crystallin.

5. Increase in the complexity of alpha-crystallins during differentiation of lens cells.

6. Hemoglobin synthesis during amphibian metamorphosis. I. Chemical studies on the hemoglobins from the larval and adult stages of Rana catesbeiana.

7. The primary structure of Golfingia gouldii hemerythrin. Oder of peptides in fragments produced by tryptic digestion of succinylated hemerythrin. Complete amino acid sequence.

8. Biochemistry of bovine lens proteins. 3. Chemical and physical properties of alpha-crystallin subunits.

9. Lactate dehydrogenase isozymes and their relationship to lens cell differentiation.

Review 1. Isoelectric focusing and immunochemistry of lens crystallins.

2. The molecular weight of the basic polypeptide chain alphaB2 of alpha-crystallin.

3. Inactive enzyme molecules in aging mice: liver aldolase.

4. The nature of the multiple forms of cytoplasmic aspartate aminotransferase from pig and sheep heart.

5. Amino acid sequences around the cysteine residue of calf lens -crystallin.

6. Acceleration of the rate of deamidation of GlyArgAsnArgGly and of human transferrin by addition of L-ascorbic acid.

7. -Crystallin. Fractionation of subunits and sequence studies on an isolated polypeptide.

8. Mechanisms of Deamidation of Asparagine Residues and Effects of Main-Chain Conformation on Activation Energy.