Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Structural studies on bovine -crystallin.

L R Croft, S G Waley

    The Biochemical Journal
    |February 1, 1971
    PubMed
    Summary
    This summary is machine-generated.

    Researchers analyzed gamma-crystallin, a lens protein, to understand its cysteine residues. This study identified eight unique cysteic acid residues, confirming a single polypeptide chain in gamma-crystallin.

    Related Concept Videos

    You might also read

    Related Articles

    Articles linked to this work by shared authors, journal, and citation graph.

    Sort by
    Same author

    Finite magnetic relaxation in x-space magnetic particle imaging: Comparison of measurements and ferrohydrodynamic models.

    Journal of physics D: Applied physics·2016
    Same author

    New potential chemotherapeutic agents; derivatives of benziminazole.

    Journal of the Chemical Society·2010
    Same author

    Site-directed mutagenesis of beta-lactamase I: role of Glu-166.

    The Biochemical journal·1994
    Same author

    Edmund Gosse and the "new and fantastic cure" for breast cancer.

    Medical history·1994
    Same author

    The kinetics of slow-binding and slow, tight-binding inhibition: the effects of substrate depletion.

    The Biochemical journal·1993
    Same author

    Site-directed mutagenesis and substrate-induced inactivation of beta-lactamase I.

    The Biochemical journal·1992
    Same journal

    Mechanistic insights into acetylated histone recognition by the CECR2 bromodomain.

    The Biochemical journal·2026
    Same journal

    Nanobodies against Plasmodium adhesins that block receptor engagement and malaria parasite invasion.

    The Biochemical journal·2026
    Same journal

    Persistence without turnover: the RhoG G12E mutant highlights the role of nucleotide cycling in RhoG signaling.

    The Biochemical journal·2026
    Same journal

    Alternative Splicing of Rice Chloroplastic CuZn Superoxide Dismutase, OsCSD2: Impact on expression and protein characteristics.

    The Biochemical journal·2026
    Same journal

    Difference and similarity between the ubiquitous secretory pathway Ca2+-ATPases, SERCA2b, and SPCA1a.

    The Biochemical journal·2026
    Same journal

    A molecular perspective on dimethylarginine dimethylaminohydrolases structure and function.

    The Biochemical journal·2026
    See all related articles

    Area of Science:

    • Biochemistry
    • Protein Chemistry
    • Ophthalmology

    Background:

    • Gamma-crystallin is a major protein in the eye lens.
    • Understanding its structure, including cysteine residues, is crucial for lens function and opacity research.

    Purpose of the Study:

    • To determine the number and location of cysteine residues in gamma-crystallin.
    • To elucidate the polypeptide chain structure of gamma-crystallin.

    Main Methods:

    • Fraction II of calf lens gamma-crystallin was oxidized with performic acid.
    • The oxidized protein was hydrolyzed using trypsin.
    • Peptides containing cysteic acid were isolated and analyzed.

    Main Results:

    • Six peptides containing cysteic acid were identified.

    Related Experiment Videos

  • One peptide contained three cysteic acid residues, while the others contained one.
  • A total of eight unique cysteic acid residues were found in the oxidized protein.

    • Conclusions:

    • Gamma-crystallin contains eight cysteine residues.
    • The amino acid analysis supports the presence of eight cysteic acid residues.
    • These findings indicate that gamma-crystallin consists of a single polypeptide chain.