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Specific Localization of Membrane Dipeptidase and Dipeptidyl Peptidase IV in Secretion Granules of Two Different Pancreatic Islet Cells

The journal of histochemistry and cytochemistry, 1999-04, Vol.47 (4), p.489-497

1999

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Identification of membrane dipeptidase as a major glycosyl-phosphatidylinositol-anchored protein of the pancreatic zymogen granule membrane, and evidence for its release by phospholipase A

Biochemical journal, 1997-05, Vol.324 ( Pt 1) (1), p.151-157

1997

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Efficient binding of regulated secretory protein aggregates to membrane phospholipids at acidic pH

Biochemical journal, 1999-03, Vol.338 ( Pt 2) (2), p.289-294

1999

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Simultaneous kinetic determinations of lipase, chymotrypsin, trypsin, elastase, and amylase on the same microtiter plate

Pancreas, 1993-05, Vol.8 (3), p.383-386

1993

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The major protein of pancreatic zymogen granule membranes (GP-2) is anchored via covalent bonds to phosphatidylinositol

Biochemical and biophysical research communications, 1988-07, Vol.154 (2), p.818-823

1988

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Membrane Dipeptidase in the Pig Exocrine Pancreas: Ultrastructural Localization and Secretion

The journal of histochemistry and cytochemistry, 1998-07, Vol.46 (7), p.841-846

1998

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Specific interactions of pancreatic amylase at acidic pH. Amylase and the major protein of the zymogen granule membrane (GP-2) bind to immobilized or polymerized amylase

Biochemistry and cell biology, 1992-10, Vol.70 (10-11), p.1105-1114

1992

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Development of GP-2 and five zymogens in the fetal and young pig: biochemical and immunocytochemical evidence of an atypical zymogen granule composition in the fetus

The journal of histochemistry and cytochemistry, 1996-05, Vol.44 (5), p.481-499

1996

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The integral and peripheral proteins of the zymogen granule membrane

Biochimica et biophysica acta, 1984-02, Vol.769 (3), p.611-621

1984

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Structure of the pig pancreatic GP-2: role of intramolecular disulfides in the resistance to proteolysis

Biochemistry and cell biology, 1989-06, Vol.67 (6), p.281-287

1989

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Identification of the catalytic subunit of the ATP diphosphohydrolase by photoaffinity labeling of high-affinity ATP-binding sites of pancreatic zymogen granule membranes with 8-azido-[alpha-32P]ATP

Biochemistry and cell biology, 1986-01, Vol.64 (1), p.13-20

1986

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Reducing conditions induce a total degradation of the major zymogen granule membrane protein in both its membranous and its soluble form. Immunochemical quantitation of the two forms

Biochemistry and cell biology, 1986-05, Vol.64 (5), p.456-462

1986

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Labeling of the proteins at the surface of the pancreatic zymogen granule using diazotized [ 125I]iodosulfanilic acid

Biochimie, 1988-02, Vol.70 (2), p.291-295

Le Bel, Denis

1988

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Specific Localization of Membrane Dipeptidase and Dipeptidyl Peptidase IV in Secretion Granules of Two Different Pancreatic Islet Cells

Identification of membrane dipeptidase as a major glycosyl-phosphatidylinositol-anchored protein of the pancreatic zymogen granule membrane, and evidence for its release by phospholipase A

Efficient binding of regulated secretory protein aggregates to membrane phospholipids at acidic pH

Simultaneous kinetic determinations of lipase, chymotrypsin, trypsin, elastase, and amylase on the same microtiter plate

The major protein of pancreatic zymogen granule membranes (GP-2) is anchored via covalent bonds to phosphatidylinositol

Membrane Dipeptidase in the Pig Exocrine Pancreas: Ultrastructural Localization and Secretion

Specific interactions of pancreatic amylase at acidic pH. Amylase and the major protein of the zymogen granule membrane (GP-2) bind to immobilized or polymerized amylase

Development of GP-2 and five zymogens in the fetal and young pig: biochemical and immunocytochemical evidence of an atypical zymogen granule composition in the fetus

The integral and peripheral proteins of the zymogen granule membrane

Structure of the pig pancreatic GP-2: role of intramolecular disulfides in the resistance to proteolysis

Identification of the catalytic subunit of the ATP diphosphohydrolase by photoaffinity labeling of high-affinity ATP-binding sites of pancreatic zymogen granule membranes with 8-azido-[alpha-32P]ATP

Reducing conditions induce a total degradation of the major zymogen granule membrane protein in both its membranous and its soluble form. Immunochemical quantitation of the two forms

Labeling of the proteins at the surface of the pancreatic zymogen granule using diazotized [ 125I]iodosulfanilic acid

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