scholarly journals Aromatic amino acid transaminase in rat intestine

1973 ◽  
Vol 135 (4) ◽  
pp. 815-818 ◽  
Author(s):  
Jun Nakamura ◽  
Tomoo Noguchi ◽  
Ryo Kido
Keyword(s):  
Amino Acids ◽  
Small Intestine ◽  
Amino Acid ◽  
Aromatic Amino Acid ◽  
Partial Purification ◽  
Rat Small Intestine ◽  
Purification And Characterization ◽  
Rat Intestine ◽  
Enzyme Preparations

The transamination of aromatic l-amino acids (5-hydroxytryptophan, tryptophan, tyrosine, phenylalanine and kynurenine) was shown to be catalysed by enzyme preparations from rat small intestine. On the basis of the partial purification and characterization of these aromatic amino acid transaminases, it is suggested that rat small intestine contains several kinds of aromatic amino acid transaminases.

Partial Purification and Characterization of Soluble Isoform of Butyrylcholinesterase from Rat Intestine

2004 ◽  
Vol 23 (2) ◽  
pp. 143-151 ◽  
Author(s):  
Özlem Yıldız ◽  
Ebru Bodur ◽  
A. Neşe Çokugraş ◽  
Nazmi Özer
Keyword(s):  
Partial Purification ◽  
Purification And Characterization ◽  
Rat Intestine

Purification and Characterization of Diamine Oxidase (Histaminase) from Rat Small Intestine

1994 ◽  
Vol 116 (3) ◽  
pp. 631-635 ◽  
Author(s):  
Hiroyuki Mizuguchi ◽  
Ikuo Imamura ◽  
Motohiko Takemura ◽  
Hiroyuki Fukui
Keyword(s):  
Small Intestine ◽  
Diamine Oxidase ◽  
Rat Small Intestine ◽  
Purification And Characterization

Mechanisms of Dipeptide Uptake by Rat Small Intestine in Vitro

1971 ◽  
Vol 40 (3) ◽  
pp. 247-259 ◽  
Author(s):  
B. Cheng ◽  
F. Navab ◽  
M. T. Lis ◽  
T. N. Miller ◽  
D. M. Matthews
Keyword(s):  
Amino Acids ◽  
Small Intestine ◽  
Amino Acid ◽  
Acid Uptake ◽  
Rat Small Intestine ◽  
Amino Acid Oxidase ◽  
Wide Range ◽  
Mucosal Cells ◽  
Hydrolysis Of

1. The uptake of l-methionine and glycine as free amino acids, and from their dipeptides by everted rings of rat small intestine in vitro has been investigated. The concentrations used covered a wide range, including values likely to be near those found in the lumen of the intestine. 2. Though no intact peptides were found in the mucosal cells, evidence was obtained which showed that hydrolysis of the peptides was cellular at all concentrations. Total hydrolysis of peptides by the intestine was very great in relation to amino acid uptake over very short incubation times, suggesting that much hydrolysis took place superficially. 3. Except at the lowest concentrations, the rates of uptake of amino acids from the peptides were more rapid than from the equivalent amino acid mixtures. Competition for uptake between glycine and methionine was avoided when they were presented in the form of l-methionylglycine. 4. Anoxia inhibited uptake of methionine from free l-methionine and from l-methionyl-l-methionine. It also inhibited hydrolysis of l-methionyl-l-methionine by intact intestine, but not by intestinal homogenates, suggesting that peptide uptake may be energy-dependent. The l-amino acid oxidase of snake venom, which destroys l-methionine but has no effect on glycine or on the peptides studied, inhibited methionine uptake from peptides when present at high concentrations, suggesting that a major site of hydrolysis is enzyme-accessible. 5. It is suggested that there may be two modes of uptake of amino acids from oligopeptides: (1) surface hydrolysis by mechanisms closely linked to the amino acid entry mechanisms, and (2) peptide entry into the mucosal cells by a special mechanism, followed by intracellular hydrolysis.

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