Fragmentation of bovine chromogranin A by plasma kallikrein.

[1]  F. Checler,et al.  Peptidasic Activities Associated with Acetylcholinesterase Are Due to Contaminating Enzymes , 1989, Journal of neurochemistry.

[2]  L. Eiden,et al.  Processing of chromogranin A within chromaffin granules starts at C‐ and N‐terminal cleavage sites , 1988, FEBS letters.

[3]  W. Dean,et al.  Calcium-binding and aggregation properties of parathyroid secretory protein-I (chromogranin A). , 1988, Bone and mineral.

[4]  H. Okayama,et al.  Primary structure of rat chromogranin A and distribution of its mRNA , 1988, FEBS letters.

[5]  N. Seidah,et al.  Structural and immunological homology of human and porcine pituitary and plasma IRCM-serine protease 1 to plasma kallikrein: marked selectivity for pairs of basic residues suggests a widespread role in pro-hormone and pro-enzyme processing. , 1988, Biochimie.

[6]  R. Angeletti,et al.  Chromogranin A-like proteins in the secretory granules of a protozoan, Paramecium tetraurelia. , 1987, The Journal of biological chemistry.

[7]  W. Huttner,et al.  The primary structure of human chromogranin A and pancreastatin. , 1987, The Journal of biological chemistry.

[8]  M. Marcinkiewicz,et al.  Chromogranin B (secretogranin I), a putative precursor of two novel pituitary peptides through processing at paired basic residues , 1987, FEBS letters.

[9]  S. Hearn.  Electron microscopic localization of chromogranin A in osmium-fixed neuroendocrine cells with a protein A-gold technique. , 1987, The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society.

[10]  D. O'Connor,et al.  Chromogranin A is present in and released by fish endocrine tissue. , 1987, Life sciences.

[11]  H. Davidson,et al.  Biosynthesis of betagranin in pancreatic beta-cells. Identification of a chromogranin A-like precursor and its parallel processing with proinsulin. , 1987, The Biochemical journal.

[12]  C. Hagn,et al.  Chromogranins A, B, and C: Widespread Constituents of Secretory Vesicles a , 1987, Annals of the New York Academy of Sciences.

[13]  D. O'Connor,et al.  How Sensitive and Specific Is Measurement of Plasma Chromogranin A for the Diagnosis of Neuroendocrine Neoplasia? a , 1987, Annals of the New York Academy of Sciences.

[14]  M. Schalekamp,et al.  Two-step prorenin-renin conversion. Isolation of an intermediary form of activated prorenin. , 1987, The Journal of biological chemistry.

[15]  J. Rossier,et al.  Chromogranin A can act as a reversible processing enzyme inhibitor , 1987, FEBS letters.

[16]  W. Huttner,et al.  Chromogranin A and pancreastatin , 1987, Nature.

[17]  L. Eiden.  Is chromogranin a prohormone? , 1987, Nature.

[18]  V. Mutt,et al.  Pancreastatin, a novel pancreatic peptide that inhibits insulin secretion , 1986, Nature.

[19]  M. Grimes,et al.  Bovine chromogranin A sequence and distribution of its messenger RNA in endocrine tissues , 1986, Nature.

[20]  D. Small,et al.  Acetylcholinesterase hydrolyses chromogranin a to yield low molecular weight peptides , 1986, Neuroscience.

[21]  J. Mallet,et al.  The primary structure of bovine chromogranin A: a representative of a class of acidic secretory proteins common to a variety of peptidergic cells. , 1986, The EMBO journal.

[22]  P. De Camilli,et al.  Secretogranins I and II: two tyrosine-sulfated secretory proteins common to a variety of cells secreting peptides by the regulated pathway , 1985, The Journal of cell biology.

[23]  N. Kitamura,et al.  Cloning and sequence analysis of cDNAs for human high molecular weight and low molecular weight prekininogens. Primary structures of two human prekininogens. , 1985, The Journal of biological chemistry.

[24]  N. Seidah,et al.  Primary structure determination of Escherichia coli heat-stable enterotoxin of porcine origin. , 1983, Canadian journal of biochemistry and cell biology = Revue canadienne de biochimie et biologie cellulaire.

[25]  L. L. Chu,et al.  Isolation and partial characterization of secretory protein I from bovine parathyroid glands. , 1981, Biochemistry.