The Glucomannan System From Aloe Vahombe (Liliaceae) III. Comparative Studies On The Glucomannan Components Isolated From The Leaves
Vilkas E; Radjabi-Nassab F
Biochimie 68(9):1123-7 1986 Sep

The polysaccharide mixture obtained by hot water extraction of Aloe vahombe leaves is composed of at least four different paritally acetylated glucomannans which differ in molecular weight, glucose to mannose ratios and acetyl contents. Furthermore, one fraction contains a small but significant amount of protein which could not be removed by gel filtration in a hydrogen-bond-breaking medium, by DEAE-Sephadex A-50 anion exchange chromatography, or by Sevag’s method.

Orientation Of Interphase Chromosomes As Detected By Giemsa C-Bands
Ghosh S; Roy SC
Chromosoma 61(1):49-55 1977 Apr 27

The orientation of Giemsa C-bands has been studied in mitotic and interphase cells of Allium cepa. A sativum and of Aloe vera. The C-bands in these three species are located at the telomeres, secondary constriction region of the nucleolar chromosomes and the centromeric regions, respectively. Observations in A. cepa and Aloe indicate clearly that the interphase chromosomes are non-random in their orientation and possibly maintain their telophase configuration through the attachment of telomeres and perhaps of kinetochores with the nuclear membrane. Electron micrographs of onion cells also reveal that certain heterochromatic segments are associated with the nuclear membrane. The nucleolar interstitial C-bands in A. sativum remain free in the nucleoplasm and may come close to each other due to heterochromatic attraction. Such a heterochromatic attraction is also evident between telomeric regions and between centromeres. However, a two by two attachment could not be noticed. A diagrammatic representation of the orientation of interphase chromosomes has been presented.

Purification Of Active Substances Of Aloe Arborescens Miller & Their Biological & Pharmacological Activity
Saito, Hiroko
Dep. Pharm., Aichi Cancer Center
Phytother Res. (1993) 7 (Spec. Issue, Proceedings of the International Congress of Phytotherapy, 1991), S14-S19

The authors purified Aloctin A from Aloe arborescens Miller and defined its chem., biol. and pharmacol. activities. Aloctin A consists of two discrete bands, a and b with a combined S-S bond. Its mol. wt. for a is 7500 and the mol. wt. for b is 10,500. Aloctin A has many biol. and pharmacol. activities as follows: 1. hemagglutinating activity; 2. cytoagglutinating activity; 3. mitogenic activity of lymphocytes; 4. ppt. - forming reactivity with a2-macroglobulin; 5. complement C3 activating activity; 6. inhibition of heat-induced hemolysis of rat erythrocytes; 7. anti-tumor effect; 8. anti-inflammatory effect; 9. inhibition of gastric secretion and gastric lesions.

The Molecular Structure Of Iso-Aloesin Isolated From The Leaves Of Aloe Vera L. Var. Chinensis (Haw.) Berge
Yuan AX
Guanxi Institute Of Traditional Chinese Medical & Pharmaceutical Sciences
Chung Kuo Chung Yao Tsa Chih (1993 Oct) 18 (10) 609-11, 639

A new constituent iso-aloesin was isolated from the leaves of Aloe vera var. chinensis found in the Province of Guangxi. The molecular formula of iso-aloesin is C19H2209, which is 2-acetonyl-6-C-beta-D-glucopyranosyl-7-hydroxy-5-methyl-chromone.

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.