
doi: 10.1007/bf02731890
A protein that inhibited the proteolytic activity of trypsin was isolated from amaranth leaves (Amaranthus cruentus) by affinity chromatography on trypsin-Sepharose. The inhibition was noncompetitive (withp-nitroanilide-N-α-benzoyl-DL-arginine as substrate) and had aK i, of 1.87 × 10−7 M. The protein caused a weaker inhibitory effect on chymotrypsin, had no effect on subtilisin, displayed a molecular weight of 8 kDa, and contained no cysteine residues.
| selected citations These citations are derived from selected sources. This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | 0 | |
| popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network. | Average | |
| influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | Average | |
| impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network. | Average |
