alpha-chymotrypsin and Galactosemias

alpha-chymotrypsin has been researched along with Galactosemias* in 2 studies

Other Studies

2 other study(ies) available for alpha-chymotrypsin and Galactosemias

ArticleYear
O-N-acetyl-D-glucosamine moiety on discrete peptide of multiple protein 4.1 isoforms regulated by alternative pathways.
    The Journal of biological chemistry, 1989, Oct-25, Volume: 264, Issue:30

    Erythrocyte protein 4.1 is a cytoplasmic protein that possesses a protein-saccharide modification structure, an O-N-acetyl-D-glucosamine (GlcNAc) moiety. We determined the amino acid sequence of the proteolytic fragment containing the O-GlcNAc moiety after labeling the saccharide with [3H]galactose in the presence of bovine milk galactosyltransferase. Glycosylation appears to occur on one or more serine or threonine residues in the following sequence: Thr-Ala-Gln-Thr-Ile-Thr-Ser-Glu-Thr-Pro-Ser-Ser-Thr-Thr-Thr-Thr-Gln-Ile-Thr-Lys . This sequence corresponds to the carboxyl-terminal half of the 34-amino acid peptide in the 22/24-kDa carboxyl-terminal domain of protein 4.1, which is one of the discrete peptides regulated by alternative RNA splicing. Multiple protein 4.1 isoforms in erythroid and nonerythroid cells including major components of erythrocyte membrane proteins, 4.1a and 4.1b, appear to contain this sequence since most immunochemically reactive proteins were labeled with [3H]galactose, with the exception of several variant polypeptides. These results appear to suggest the functional or biological significance of the O-GlcNAc linkage in protein 4.1.

    Topics: Acetylglucosamine; Amino Acid Sequence; Animals; Chromatography, Ion Exchange; Chymotrypsin; Cytoskeletal Proteins; Electrophoresis, Polyacrylamide Gel; Erythrocyte Membrane; Galactosemias; Glucosamine; Glycopeptides; Glycosylation; Humans; Membrane Proteins; Molecular Sequence Data; Molecular Weight; Neuropeptides; Peptide Fragments; Peptide Mapping

1989
The role of sialic acid and galactose residues in determining the survival of human plasma alpha-antitrypsin in the blood circulation.
    Archives of biochemistry and biophysics, 1977, Volume: 179, Issue:2

    Topics: alpha 1-Antitrypsin; Carbohydrates; Chymotrypsin; Drug Stability; Galactosemias; Half-Life; Humans; Immunodiffusion; Kidney; Kinetics; Liver; Lung; Neuraminidase; Organ Specificity; Sialic Acids; Trypsin Inhibitors

1977