Pharmacologically Active Ingredients III

A Phytochemical Study Of Aloe Vera Leaf Rowe, Tom D; Parks, Lloyd M Journal of the American pharmaceutical Assoction 1939 Vol 21 pp. 538-539 In 1939, professor Tom D. Row, Lloyd M. Parks, and associates made a breakdown of Aloe vera which would prove to be the most extensive to that time. Believing that the real curative properties would be found in the rind rather than the gel, Rowe and Parks isolated the following components: the hydrolyzing enzymes oxydase, catalase, and amylase; beta carotene (a pro-vitamin of vitamin A); the starch-splitting enzyme, pentosan; calcium oxalate; a mineral based cleansing agent. They also isolated many of the anthraquinones discovered earlier by Chopia and Gosh as well as traces of other vitamins and minerals. Biological Activity Of Aloe Vera Davis, Robert H Dep. Biomed. Sci., Pennsylvania Coll. Podiatr. Med. Seifen, Oele, Fette, Wachse (1993) 119(11), 646, 648-9 Some of the constituents of Aloe vera (AV) have biol. activity similar to amino acids, vitamin C and growth factors like gibberellin and auxin. The AV mol. probably does not act alone, but rather acts in either an additive or synergistic fashion with some of the 100 constituents of the AV. Glyoxalase I & Glyoxalase II From Aloe Vera: Purification, Characterization & Comparison With Animal Glyoxalases Norton SJ; Talesa V; Yuan WJ; Principato GB Department Of Biochemistry, University Of North Texas Biochem Int 22(3):411-8 1990 Nov Glyoxalase I and glyoxalase II from the outer green rind of Aloe vera leaves were purified by (matrix) affinity ligand-enzyme binding methods. The purified enzymes exhibited single protein bands on SDS-PAGE electrophoresis, with MW values of approximately 44,000 and 27,000 for glyoxalase I and glyoxalase II, respectively. The glyoxalase I is a basic protein (pI 7.8), while the glyoxalase II (3 protein bands) is acidic (pI 4.7, 4.8 [prevalent form], and 5.0). The kinetic constants, Km and Vmax, and Ki values for certain inhibitors are reported for both glyoxalase I and glyoxalase II. The glyoxalase enzymes from Aloe vera were compared with reported animal and plant glyoxalases. Antibradykinin Active Material In Aloe Saponaria Yagi A; Harada N; Yamada H; Iwadare S; Nishioka I J Pharm Sci 71(10):1172-4 1982 Oct A material having antibradykinin activity on isolated guinea pig ileum was partially purified from the nondialysate of the pulp of Aloe saponaria by repetition of gel chromatography using a hydrophilic polyvinyl gel and dextran gels. From the results of amino acid and carbohydrate analyses, the antibradykinin-active material was estimated to be a glycoprotein. It was found that this material catalyzes the hydrolysis of bradykinin at pH 7.4. The results of peptide analysis using reversed-phase high-performance liquid chromatography coupled with amino acid analysis indicate that this glycoprotein cleaves the Gly4-Phe5 and Pro7-Phe8 bonds of the bradykinin molecule.