Dipeptidase deficiency and malabsorption of glycylglycine in disease states

Sadikali, F.

doi:10.1136/gut.12.4.276

Cited by 37 publications

(16 citation statements)

References 32 publications

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“…In the guinea-pig also, only 5-10% of dipeptidase activity is present in the brush-border region and the remainder is in the cytosol (Peters, 1970). It seems possible that this subject had a deficiency of glycylglycine dipeptidase (Sadikali, 1971). One subject in the present study had very low absorption rates for both glycine and glycylglycine; the reason is not clear.…”

Section: Discussioncontrasting

confidence: 50%

Comparison of Intestinal Absorption Rates of Glycine and Glycylglycine in Man and the Effect of Glucose in the Perfusing Fluid

Cook

1972

Clinical Science

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S U M M A R Y1. Using a double-lumen tube perfusion system the rates of glycine, glycylglycine, and glycylglycine and glucose absorption from a 30-cm jejunal segment have been studied in vivo in a group of relatively normal Zambian African subjects.2. To determine the kinetic curve for glycine absorption, four subjects were given consecutive perfusions of 50, 100 and I50 m-glycine.3. Six other subjects had consecutive perfusions of (1) a 100 mwglycine and (2) a 50 mM-glycylglycine solution. Five of the six had a higher absorption rate of glycine from the glycylglycine solution. When data from a further six similar subjects in another study are included, the mean rate of glycine absorption is significantly greater from the glycylglycine compared with h e glycine solution (P

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Section: Discussioncontrasting

confidence: 50%

Comparison of Intestinal Absorption Rates of Glycine and Glycylglycine in Man and the Effect of Glucose in the Perfusing Fluid

Cook

1972

Clinical Science

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“…However it is not yet clear whether dietary protein is absorbed from intestinal lumen to mucosa primarily as amino acids or as small peptides. Several studies have recently shown that certain dipeptides and tripeptides may be absorbed as efficiently or even more efficiently than the constituent amino acids, suggesting that the dietary protein may be absorbed in both forms (8)(9)(10)(11). Though peptide hydrolases of the small intestine are generally thought to play an important role in the final step of the digestion of dietary proteins, little is known of the subcellular fraction most concerned with this activity; furthermore the possible role of dipeptidases in other cellular functions has not been examined.…”

Section: Introductionmentioning

confidence: 99%

Peptide hydrolases in the brush border and soluble fractions of small intestinal mucosa of rat and man

Kim¹,

Birtwhistle²,

Kim³

1972

J. Clin. Invest.

159

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A BST RA CT Peptide hydrolases, catalyzing the hydrolysis of 13 dipeptides and 5 tripeptides into their respective amino acids, were studied in small intestinal mucosa and other tissues, in man and in the rat.Studies on the subcellular distribution of these enzymes showed enzyme activities in both the soluble and brush border fractions of the rat small intestinal mucosa, the former constituting 80-90% and the latter 10-15% of the total activity. Zymogram studies of peptide hydrolases, in both fractions, yielded multiple bands indicating multiple zones of enzyme activity. With most substrates a rather broad range of enzyme activities was observed in the soluble fraction differing only slightly from substrate to substrate, the exception being when L-leucyl-L-proline was used: this latter led to a zymogram pattern which was quite distinct. The synthetic substrates, L-leucyl-P-naphthylamide and Lleucinamide appeared to be hydrolyzed by two electrophoretically distinct enzymes, different from those hydrolyzing other leucyl-containing peptide substrates.Zymogram patterns of the brush border membrane fraction were quite different from those of the soluble fraction of rat small intestine indicating that enzymes from the two sources may be different. No comparable human data were obtained.Peptide hydrolases in the soluble fractions of various organs from the same species gave similar zymogram patterns, while those from the plasma membrane-bound fractions of different organs in the same species were peculiar to each organ. From these data, it is suggested that peptide hydrolases in the brush border and the soluble fractions of small intestine are distinct enzymes and may play different roles in cellular function.

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“…As for intestinal enzymes, it is known that severe, persistent lactase deficiency causes lactose intolerance (Bolin and Davis, 1972 ;Kretchmer, 1971). Sadikali (1971) …”

mentioning

confidence: 99%

The adaptation of digestive enzymes to the diet : Its physiological significance

Corring¹

1980

Reprod. Nutr. Dévelop.

123

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Dipeptidase deficiency and malabsorption of glycylglycine in disease states

Cited by 37 publications

References 32 publications

Comparison of Intestinal Absorption Rates of Glycine and Glycylglycine in Man and the Effect of Glucose in the Perfusing Fluid

Comparison of Intestinal Absorption Rates of Glycine and Glycylglycine in Man and the Effect of Glucose in the Perfusing Fluid

Peptide hydrolases in the brush border and soluble fractions of small intestinal mucosa of rat and man

The adaptation of digestive enzymes to the diet : Its physiological significance

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