The Significance of Gelatin Tolerance in Malabsorptive States

Bronstein, Howard D.; Haeffner, Lorraine J.; Kowlessar, O. Dhodanand

doi:10.1016/s0016-5085(66)80119-1

Cited by 26 publications

(5 citation statements)

References 10 publications

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“…Pyrrolidone carboxylyl peptides, present in the other fractions (mainly fraction 1) and previously thought (Bronstein, Haeffner, and Kowlessar, 1966) to be toxic in coeliac disease, did not affect D-xylose excretion. This is in keeping with the results of our mucosal digestion experiments (Cornell and Townley, 1973) and those of Woodley (1972) who showed no deficiency of pyrrolidone carboxylyl peptidase in coeliac intestinal mucosa.…”

Section: Wheat Gliadinmentioning

confidence: 65%

The toxicity of certain cereal proteins in coeliac disease

Cornell¹,

Townley²

1974

Gut

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SUMMARY Gliadins from wheat, rye, and oats, and from wheat glutenin were digested with pepsin, trypsin, and pancreatin and the products (PTC digests) chromatographed on sulphopropyl (SP) Sephadex.Fractions eluted near neutral pH from wheat, rye, and oats gliadin digests all had very similar amino acid composition, although the oats fraction was higher in sulphur-containing amino acids. The major amino acids present in all were glutamine/glutamic acid and proline.The amount of fraction eluted near neutral pH from oats gliadin digest was about 13 % of that eluted from digests of wheat and rye gliadins. Moreover, the yield of gliadin from oatmeal was only 0 5 % compared with 2.4 % and 2.8 % from rye and wheat flours respectively.The amount of fraction eluted from wheat glutenin digest was about 70 % of that obtained from wheat and rye gliadin digests.The fractions eluted near neutral pH from all protein digests were defectively digested by remission coeliac mucosa, and D-xylose excretion tests with the fraction from the wheat gliadin digest (fraction 9) indicated that it is harmful to subjects with coeliac disease, whereas the other fractions of this digest gave no such evidence.The results of the present work indicate that counterpart fractions to fraction 9 obtained from wheat glutenin and rye and oats gliadins may also be important in the aetiology of coeliac disease.

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Section: Wheat Gliadinmentioning

confidence: 65%

The toxicity of certain cereal proteins in coeliac disease

Cornell¹,

Townley²

1974

Gut

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“…As might be expected, absorption is poor when whole protein is given, but absorption of free amino acids is normal (Christensen and Shwachman, 1949;Anfanger and Heavenrich, 1949;Chinn, Lavik, Babb, Buckaloo. Stitt, and Abbott, 1953;Richmond and Girdwood, 1962;Laster and Matthews, 1963;Bronstein et al, 1966;.…”

Section: Malhbsorption Of Proteinsmentioning

confidence: 99%

Protein absorption

Matthews¹

1971

Journal of Clinical Pathology

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In the last 20 years, the mechanisms of protein absorption have been studied with increasing intensity, and a large book could be written on this subject alone. In spite of this volume of work, it has recently become clear that our knowledge of protein absorption is still far from complete, since until very recently nearly all investigations have been concerned with the intestinal transport of amino acids. Evidence for the existence of a second important mode of protein absorption-mucosal uptake of small peptides with cellular hydrolysis-is now extremely strong, and the importance of this mode of absorption is maintaining nutrition in cases of intestinal transport defects for amino acids has recently been demonstrated. Yet the details of mucosal oligopeptide transport have hardly begun to be explored. It is therefore difficult to give a balanced account of protein absorption at the present time. This account is selective, most attention being paid to growing points in the field. Several reviews covering the details of amino-acid absorption are available (Wilson

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“…Gelatin contains about 14"', of hydroxyproline, which is absorbed following digestion as a mixture of short peptides, an amount proportional to blood levels being excreted in the urine (Prockop et al, 1962). At the end of each test month the patient was put on a lolls gelatin diet (Bronstein et al, 1966;Cerda et al, 1968) and after completion of a basal 24-hour urine collection 25 g. of Dowdered gelatin (B.P.) in water was drunk immediately after taking the P.I)propriate dose of trial tablets.…”

Section: Fat Analysis and Gelatin Tolerance Testmentioning

confidence: 99%

Comparative Trial of Nutrizym in Chronic Pancreatic Insufficiency

Knill‐Jones¹,

Pearce²,

Batten³

et al. 1970

BMJ

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Summary: A cross-over trial of pancreatic replacement therapy was carried out in 12 adults with chronic pancreatic insufficiency. The standard enteric-coated preparation, Pancrex V forte, was compared with Nutrizym, which has an enteric-coated core of pancreatic extract and a shell of bromelains-a mixture of proteolytic enzymes derived from the stem of the pineapple.Nutrizym was significantly more effective than Pancrex V forte in improving fat absorption, and reduced faecal weight. Protein digestion was assessed by measuring the urinary excretion of hydroxyproline after a gelatin meal. Nutrizym produced an earlier and significantly higher peak in hydroxyproline excretion than Pancrex V forte, but the cumulative effect was similar. The value of bromelains was investigated by including a period on the Nutrizym core alone. This was similar to Pancrex V forte in improving fat absorption but had less effect on protein digestion, suggesting that the beneficial effect of Nutrizym compared with Pancrex V forte was due to the added bromelains, and not to differences in enzyme content or enteric coating.

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The Significance of Gelatin Tolerance in Malabsorptive States

Cited by 26 publications

References 10 publications

The toxicity of certain cereal proteins in coeliac disease

The toxicity of certain cereal proteins in coeliac disease

Protein absorption

Comparative Trial of Nutrizym in Chronic Pancreatic Insufficiency

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