In short-term feeding experiments, about 78% of the phaseolin administered to rats was degraded regardless of the amounts of phaseolin intubated. In contrast, the total N found in the feces increased rapidly and exceeded the original administered amounts. The bulk of N output was not immunologically related to the glycoprotein. The effects of phaseolin on the stimulation of endogenous N secretion in the small intestine were confirmed from the results of acute experiments. Phaseolin fragments, derived from the breakdown of the native protein, when reapplied intragastrically to rats, were broken down further and to a similar extent as the original glycoprotein and were even more potent related to stimulation of N secretion. It is suggested that this secretagogue biological activity of phaseolin and not its resistance to gut proteolysis, is the main reason for the poor nutritional value of this glycoprotein.
It has been reported that Coffea arabica seeds contain as the main reserve protein, a legumin-like protein, constituted of two subunits, alpha and beta, of approximately 35 and 20 kDa. In this work the seed proteins of several coffee species and varieties were investigated by SDS-PAGE and gel filtration. No differences were observed in the electrophoretic profiles among varieties of C. arabica, however, marked differences were observed among species, or even among individuals of some species. In general, the molecular weight of the subunits alpha and beta accounted for a monomer of 48 to 62 kDa. However, native molecular weight obtained by gel filtration showed that for most of the species there is association of 6 of such proteins, in a hexamer. The most marked difference was observed for C. canephora and C. racemosa. The former clearly showing isoforms of the subunits, and the later showing absence of the beta subunit. The influence of proteases in this observations is discussed.
Rats fed a diet containing a highly purified preparation of phaseolin, the main globulin from the seeds of Phaseolus vulgaris, rapidly lost weight. Fecal nitrogen outputs were elevated and the N digestibility, based on conventional method estimation, was only 37.5%. By using immunological techniques, however, it was shown that the bulk of the nitrogen recovered in the feces was not chemically related to phaseolin. After correction for this non-phaseolin N, the true digestibility of phaseolin was estimated to be 74.3%. It is suggested that phaseolin and/or undigested fragments derived from the native molecule may, as reported for the lectins, stimulate the secretion of endogenous N, possibly mucins.
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