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. 1973 Jul;52(7):1660–1664. doi: 10.1172/JCI107346

Trypsin-Like Nature of the Pancreatic Factor That Corrects Vitamin B12 Malabsorption Associated with Pancreatic Dysfunction

Phillip P Toskes 1,2, Julius J Deren 1,2, Marcel E Conrad 1,2
PMCID: PMC302440  PMID: 4718958

Abstract

Hog pancreas was subfractionated and assessed for its ability to correct vitamin B12 malabsorption in patients with pancreatic dysfunction and in rats with partial pancreatic extirpation. The constituent obtained from the pancreas that increased vitamin B12 absorption in both humans and rats was soluble at 50,000 g, heat labile, acid stable, and approximately 20,000-25,0000 in molecular weight. The active subfractions contained tryptic and chymotryptic but no amylase or lipase activity. Thrice-crystallized trypsin corrected the vitamin B12 malabsorption in both patients with pancreatic insufficiency and in rats with subtotal pancreatectomy. These data indicate that pancreatic proteolytic enzymes—in particular, trypsin—are necessary for optimal vitamin B12 absorption.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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