pituitrin and glycine-amide

pituitrin has been researched along with glycine-amide* in 2 studies

Other Studies

2 other study(ies) available for pituitrin and glycine-amide

Article	Year
Catalytic cleavage of vasopressin by human Bence Jones proteins at the arginylglycinamide bond. Biological chemistry, 1996, Volume: 377, Issue:9 Bence Jones proteins were capable of hydrolyzing a peptide bond between arginine-8 and the C-terminal glycinamide of vasopressin. This peptidolytic activity obeyed typical Michaelis-Menten kinetics and exhibited optimal activity at pH 8.2 and Km of 0.6-1.9 mM. The catalytic efficiency, kcat/Km, was calculated to be 0.8 to 5.8 min(-1)M(-1). The Bence Jones proteins displayed turnover, an essential feature of enzymes. These results suggest that slow proteolysis, especially in the renal tubules which are 'saturated' with Bence Jones proteins, may have a pathophysiological significance for various nephropathies often associated with multiple myeloma with Bence Jones proteinuria. Topics: Arginine; Bence Jones Protein; Catalysis; Glycine; Humans; Hydrogen-Ion Concentration; Hydrolysis; Kinetics; Multiple Myeloma; Vasopressins	1996
The vasopressin precursor in the Brattleboro (di/di) rat. International journal of peptide and protein research, 1988, Volume: 32, Issue:6 The vasopressin precursor in the rat hypothalamus has been studied, using trypsin to release desglycinamide vasopressin and coupling it to glycinamide (T & G treatment). The resulting amidated nonapeptide was detected and measured with a radioimmunoassay for vasopressin. The "vasopressin" produced in this way had the full immunoreactivity of the authentic peptide but eluted from an hplc column 1 min earlier and appeared to have a larger molecular weight. It was found that T&G treatment generated vasopressin immunoreactivity in extracts of the supraoptic nucleus (SON) of the Brattleboro rat in just the same way as it did in normal animals. Furthermore, this procedure produced vasopressin immunoreactivity in those hplc fractions from Brattleboro SON extracts that corresponded with the elution time of vasopressin precursor. Similar amounts of "vasopressin" could be generated from Brattleboro and normal SONs. These results support the suggestion that the Brattleboro SON synthesizes an aberrant vasopressin precursor which is not processed by the cell. Topics: Animals; Arginine Vasopressin; Brain; Glycine; Male; Neurophysins; Oxytocin; Pituitary Gland; Protein Precursors; Protein Processing, Post-Translational; Radioimmunoassay; Rats; Rats, Brattleboro; Rats, Mutant Strains; Trypsin; Vasopressins	1988

Article

Year

Catalytic cleavage of vasopressin by human Bence Jones proteins at the arginylglycinamide bond.

Biological chemistry, 1996, Volume: 377, Issue:9

Bence Jones proteins were capable of hydrolyzing a peptide bond between arginine-8 and the C-terminal glycinamide of vasopressin. This peptidolytic activity obeyed typical Michaelis-Menten kinetics and exhibited optimal activity at pH 8.2 and Km of 0.6-1.9 mM. The catalytic efficiency, kcat/Km, was calculated to be 0.8 to 5.8 min(-1)M(-1). The Bence Jones proteins displayed turnover, an essential feature of enzymes. These results suggest that slow proteolysis, especially in the renal tubules which are 'saturated' with Bence Jones proteins, may have a pathophysiological significance for various nephropathies often associated with multiple myeloma with Bence Jones proteinuria.

Topics: Arginine; Bence Jones Protein; Catalysis; Glycine; Humans; Hydrogen-Ion Concentration; Hydrolysis; Kinetics; Multiple Myeloma; Vasopressins

1996

The vasopressin precursor in the Brattleboro (di/di) rat.

International journal of peptide and protein research, 1988, Volume: 32, Issue:6

The vasopressin precursor in the rat hypothalamus has been studied, using trypsin to release desglycinamide vasopressin and coupling it to glycinamide (T & G treatment). The resulting amidated nonapeptide was detected and measured with a radioimmunoassay for vasopressin. The "vasopressin" produced in this way had the full immunoreactivity of the authentic peptide but eluted from an hplc column 1 min earlier and appeared to have a larger molecular weight. It was found that T&G treatment generated vasopressin immunoreactivity in extracts of the supraoptic nucleus (SON) of the Brattleboro rat in just the same way as it did in normal animals. Furthermore, this procedure produced vasopressin immunoreactivity in those hplc fractions from Brattleboro SON extracts that corresponded with the elution time of vasopressin precursor. Similar amounts of "vasopressin" could be generated from Brattleboro and normal SONs. These results support the suggestion that the Brattleboro SON synthesizes an aberrant vasopressin precursor which is not processed by the cell.

Topics: Animals; Arginine Vasopressin; Brain; Glycine; Male; Neurophysins; Oxytocin; Pituitary Gland; Protein Precursors; Protein Processing, Post-Translational; Radioimmunoassay; Rats; Rats, Brattleboro; Rats, Mutant Strains; Trypsin; Vasopressins

1988