Processing of the propeptide form of rat renal γ‐glutamyltranspeptidase

[1]  D. Wagner,et al.  Biosynthesis of von Willebrand protein by human endothelial cells. Identification of a large precursor polypeptide chain. , 1983, The Journal of biological chemistry.

[2]  N. Katunuma,et al.  Structural studies of the carbohydrate moieties of rat kidney gamma-glutamyltranspeptidase. An extremely heterogeneous pattern enriched with nonreducing terminal N-acetylglucosamine residues. , 1983, The Journal of biological chemistry.

[3]  J. Brunner,et al.  Isolation of the hydrophobic membrane binding domain of rat renal gamma-glutamyl transpeptidase selectively labeled with 3-trifluoromethyl-3-(m-[125I]iodophenyl)diazirine. , 1982, The Journal of biological chemistry.

[4]  N. Curthoys,et al.  Evidence that the hydrophobic domain of rat renal gamma-glutamyltransferase spans the brush border membrane. , 1982, Biochimica et biophysica acta.

[5]  J. Habener,et al.  Cellular and cell-free processing of parathyroid secretory proteins. , 1982, The Journal of biological chemistry.

[6]  S. Tate,et al.  Biosynthesis of rat renal gamma-glutamyl transpeptidase. Evidence for a common precursor of the two subunits. , 1982, The Journal of biological chemistry.

[7]  M. Reitman,et al.  Lysosomal enzyme targeting. N-Acetylglucosaminylphosphotransferase selectively phosphorylates native lysosomal enzymes. , 1981, The Journal of biological chemistry.

[8]  G. Blobel,et al.  Biosynthesis of a lysosomal enzyme. Partial structure of two transient and functionally distinct NH2-terminal sequences in cathepsin D. , 1981, The Journal of biological chemistry.

[9]  N. Curthoys,et al.  The absolute asymmetry of orientation of gamma-glutamyltranspeptidase and aminopeptidase on the external surface of the rat renal brush border membrane. , 1980, Journal of Biological Chemistry.

[10]  C. Gahmberg,et al.  Effect of tunicamycin on the biosynthesis of the major human red cell sialoglycoprotein, glycophorin A, in the leukemia cell line K562. , 1980, The Journal of biological chemistry.

[11]  N. Curthoys,et al.  The interorgan metabolism of glutathione. , 1980, The International journal of biochemistry.

[12]  W. Lennarz.  The Biochemistry of Glycoproteins and Proteoglycans , 1980, Springer US.

[13]  J. Tang,et al.  Cathepsin D isozymes from porcine spleens. Large scale purification and polypeptide chain arrangements. , 1979, The Journal of biological chemistry.

[14]  N. Curthoys,et al.  Comparison of the association and orientation of gamma-glutamyltranspeptidase in lecithin vesicles and in native membranes. , 1979, The Journal of biological chemistry.

[15]  Y. Morino,et al.  Affinity labeling of rat-kidney gamma-glutamyl transpeptidase. , 1977, European journal of biochemistry.

[16]  A. Meister,et al.  Affinity labeling of gamma-glutamyl transpeptidase and location of the gamma-glutamyl binding site on the light subunit. , 1977, Proceedings of the National Academy of Sciences of the United States of America.

[17]  W. Lennarz,et al.  Enzymatic conversion of proteins to glycoproteins. , 1977, Proceedings of the National Academy of Sciences of the United States of America.

[18]  N. Curthoys,et al.  Comparison of the size and physical properties of gamma-glutamyltranspeptidase purified from rat kidney following solubilization with papain or with Triton X-100. , 1976, The Journal of biological chemistry.

[19]  R. Laskey,et al.  Quantitative film detection of 3H and 14C in polyacrylamide gels by fluorography. , 1975, European journal of biochemistry.

[20]  U. K. Laemmli,et al.  Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 , 1970, Nature.