By Irvin E. Liener
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Extra resources for Toxic constituents of plant foodstuffs
The latter could then be dissociated from this insoluble complex by elution with 6 M urea. The inhibitor was further purified by chromatography on CM-cellulose and Sephadex G-75. The purified inhibitor was found to have a molecular weight of about 20,000 with the amino acid composition shown in Table III. Serine and isoleucine constitute the N-terminal and C-terminal residues of the intact inhibitor respectively. It is important to note that the inhibitor isolated by this procedure has been modified by virtue of the tryptic cleavage of an arginine-leucine bond (see Section VI for further discussion).
The molecular weights of these four fractions was within the range of 8000-10,000, and they all had similar amino acid compositions (Table III) with cystine values of 17-20%. Ferdinand et al. (1965) found that the relative proportions of each of these active components varied with different commercial preparations of the lima bean inhibitor and with different varieties of beans. These authors suggested that these inhibitors most likely represent a family of closely related polypeptides arising as a result of enzymatic action on a single precursor in the bean or the manifestation of genetic heterogeneity.
It was established that inhibitor A was derived from inhibitor B as a result of deamination produced by treatment with trichloroacetic acid during the isolation procedure. Estimates of the molecular weight of inhibitor A based on amino acid composition (Table III), osmotic pressure, sedimentation, and gel filtration gave values between 8000 — 9000. 2%) is significantly less, and corresponds to 4 disulfide bonds. D. Phaseolus vulgaris The large number of varieties of beans which are classified as Phaseolus vulgaris makes it rather difficult to compare the data of investigators who have studied protease inhibitors from different varieties of this legume.
Toxic constituents of plant foodstuffs by Irvin E. Liener