High and low inhibitor soybean meals affect human duodenal proteinase activity differently: in vivo comparison with bovine serum albumin
H Holm, LE Hanssen, Å Krogdahl, J Florholmen - The Journal of nutrition, 1988 - Elsevier
The objective of this study was to investigate the effects of high and low inhibitor soybean
meals on the duodenal enzyme activities and on the possible regulatory role of
gastrointestinal hormones in the pancreatic response. After an overnight fast, 11 healthy
volunteers received an intraduodenal infusion of saline for 60 min. This was followed by
infusion of either of three test meals: extract of raw soybeans (RS), a low inhibitor soy protein
isolate (SPI) or bovine serum albumin (BSA), 10 g/h for 60 min. Then saline was again given …
meals on the duodenal enzyme activities and on the possible regulatory role of
gastrointestinal hormones in the pancreatic response. After an overnight fast, 11 healthy
volunteers received an intraduodenal infusion of saline for 60 min. This was followed by
infusion of either of three test meals: extract of raw soybeans (RS), a low inhibitor soy protein
isolate (SPI) or bovine serum albumin (BSA), 10 g/h for 60 min. Then saline was again given …
High and low inhibitor soybean meals affect human duodenal proteinase activity differently: in vitro comparison of proteinase inhibition
H Holm, Å Krogdahl, LE Hanssen - The Journal of nutrition, 1988 - Elsevier
The purpose of the study was to investigate the in vitro inhibition of the proteolytic activity in
samples of duodenal juice obtained during instillation of raw soybeans in humans. The
results suggested the presence of an inhibitor-resistant trypsin. Practically no inhibition was
obtained with phenylmethylsulfonyl fluoride, aprotinin, human α 1-antitrypsin or lima bean
trypsin inhibitor. Specificity against synthetic substrates was different from that obtained in
the absence of raw soybeans. Duodenal aspirates containing this new trypsin activity were …
samples of duodenal juice obtained during instillation of raw soybeans in humans. The
results suggested the presence of an inhibitor-resistant trypsin. Practically no inhibition was
obtained with phenylmethylsulfonyl fluoride, aprotinin, human α 1-antitrypsin or lima bean
trypsin inhibitor. Specificity against synthetic substrates was different from that obtained in
the absence of raw soybeans. Duodenal aspirates containing this new trypsin activity were …
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