somatostatin--n-tyr(1)- and Stomach-Neoplasms

somatostatin--n-tyr(1)- has been researched along with Stomach-Neoplasms* in 1 studies

Other Studies

1 other study(ies) available for somatostatin--n-tyr(1)- and Stomach-Neoplasms

Article	Year
[Purification to apparent homogeneity of the somatostatin receptor of the human cell line HGT-1 of gastric origin]. Comptes rendus de l'Academie des sciences. Serie III, Sciences de la vie, 1989, Volume: 308, Issue:9 This communication reports the isolation and the purification of the gastric somatostatin receptor from the human cell line HGT-1. The receptor has been extracted from the cell membrane by Triton X 100, and a monoclonal antibody to this was prepared. A series of affinity chromatographies (Sepharose-antibody and Sepharose-somatostatin-14) and a final purification by steric exclusion on high performance liquid chromatography columns (HPLC) allowed us to obtain a fraction enriched 20,000 fold in 125I-Tyrll-somatostatin-14 specific binding (apparent dissociation constant: 7.6 x 10(-8) M). This fraction corresponded to a molecular mass of about 90 kDa (in presence of detergent) and to a maximal binding capacity of more than 10,000 pmol/protein. It therefore has a theoretical homogeneity close to 100%. Topics: Cell Membrane; Chromatography, Affinity; Chromatography, High Pressure Liquid; Humans; Immunoblotting; Immunoenzyme Techniques; Molecular Weight; Receptors, Neurotransmitter; Receptors, Somatostatin; Somatostatin; Stomach Neoplasms; Tumor Cells, Cultured	1989

Article

Year

[Purification to apparent homogeneity of the somatostatin receptor of the human cell line HGT-1 of gastric origin].

Comptes rendus de l'Academie des sciences. Serie III, Sciences de la vie, 1989, Volume: 308, Issue:9

This communication reports the isolation and the purification of the gastric somatostatin receptor from the human cell line HGT-1. The receptor has been extracted from the cell membrane by Triton X 100, and a monoclonal antibody to this was prepared. A series of affinity chromatographies (Sepharose-antibody and Sepharose-somatostatin-14) and a final purification by steric exclusion on high performance liquid chromatography columns (HPLC) allowed us to obtain a fraction enriched 20,000 fold in 125I-Tyrll-somatostatin-14 specific binding (apparent dissociation constant: 7.6 x 10(-8) M). This fraction corresponded to a molecular mass of about 90 kDa (in presence of detergent) and to a maximal binding capacity of more than 10,000 pmol/protein. It therefore has a theoretical homogeneity close to 100%.

Topics: Cell Membrane; Chromatography, Affinity; Chromatography, High Pressure Liquid; Humans; Immunoblotting; Immunoenzyme Techniques; Molecular Weight; Receptors, Neurotransmitter; Receptors, Somatostatin; Somatostatin; Stomach Neoplasms; Tumor Cells, Cultured

1989