Experimental approach in chemical pathology.

Matthews, D. M.

doi:10.1136/bmj.3.5776.659

Cited by 9 publications

(2 citation statements)

References 35 publications

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“…Investigations of absorption of free amino acids and dipeptides by means of tolerance tests and transport studies in a jejunal biopsy have provided additional evidence for retention of the ability to take up dipeptides in the presence of an amino acid transport defect. Some of the results have already been briefly reported (Tarlow et al, 1970;Matthews, 1971b).…”

mentioning

confidence: 90%

Absorption of Amino Acids and Peptides in a Child with a Variant of Hartnup Disease and Coexistent Coeliac Disease

Tarlow¹,

Seakins²,

Lloyd³

et al. 1972

Archives of Disease in Childhood

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mentioning

confidence: 90%

Absorption of Amino Acids and Peptides in a Child with a Variant of Hartnup Disease and Coexistent Coeliac Disease

Tarlow¹,

Seakins²,

Lloyd³

et al. 1972

Archives of Disease in Childhood

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“…In view of the importance of peptide hydrolases of the small intestinal mucosa in the final phases of protein digestion (Newey and Smyth, 1960;Crane, 1961;Rhodes, Eichholz, and Crane, 1967;Matthews, 1971), we have studied the intestinal carnosinase of the rat and of the human subject in both normal and various disease states. The role of this dipeptidase for absorption of L-carnosine was tested by comparing the tolerance curves for the dipeptide and its constituent amino acids in two patients, one of whom had a markedly reduced activity of jejunal carnosinase.…”

mentioning

confidence: 99%

Carnosinase activity of human gastrointestinal mucosa.

Sadikali¹,

Darwish²,

Watson³

1975

Gut

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SUMMARY Carnosinase, the dipeptidase which hydrolyses carnosine and other histidine-containing dipeptides, was assayed in mucosal tissues of the human and of the rat gut. Kinetic properties of the intestinal enzyme were found to be similar to carnosinase of other animal tissues. Little or no activity was detected in human gastric or colonic mucosa, and the levels were lower in duodenal than jejunal mucosa. The distribution of carnosinase is similar to that of the disaccharidases. Mean carnosinase activity was 8'8 units/g weight in 15 patients with histologically normal mucosa compared with 5-7 units in five with villous atrophy. The enzyme levels increased with histological improvement of the mucosa in patients with coeliac disease on a gluten-free diet. Tolerance curves for carnosine and its constitutent amino acids showed malabsorption of the dipeptide in a patient with carnosinase deficiency. It is concluded that the intestinal mucosa has much less hydrolase activity for carnosine than for glycylglycine and other dipeptidases, and the relatively slow hydrolysis appears to be the rate-limiting step in the total absorptive process.

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Rates of Peptide Uptake by Small Intestine

Dm¹

1972

Ciba Foundation Symposium 4 ‐ Peptide Transport in Bacteria and Mammalian Gut

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Experimental approach in chemical pathology.

Cited by 9 publications

References 35 publications

Absorption of Amino Acids and Peptides in a Child with a Variant of Hartnup Disease and Coexistent Coeliac Disease

Absorption of Amino Acids and Peptides in a Child with a Variant of Hartnup Disease and Coexistent Coeliac Disease

Carnosinase activity of human gastrointestinal mucosa.

Rates of Peptide Uptake by Small Intestine

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