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Biomedical subjects

D Borovsky

Publications and source records attributed to D Borovsky.

28 records · Page 2Linked to original sources

Trypsin and chymotrypsin-like enzymes of the sandfly Phlebotomus papatasi infected with Leishmania and their possible role in vector competence.

Phlebotomus papatasi (Scopoli) is susceptible to infection with Leishmania major Yakimov & Schokov and resistant to L. donovani Laveran & Mesnil. The possibility that susceptibility depends on midgut levels of trypsin and chymotrypsin-like (esterolytic) enzymes was investigated. Infection with L. major reduced the trypsin-like activity to 93.5% and 86% of the control value at 20 and 30 h post feeding and increased it to 106% at 52 h. Infection with L. donovani reduced trypsin-like activity to 64% and 73% of the control value at 30 and 52 h post feeding. The overall amount of trypsin and chymotrypsin-like enzymes in L. major infections was reduced to 50% and 34% of the control value at 20 and 30 h post feeding and increased to 184% at 52 h. Only one of the enzymes separated by gel electrophoresis was lower throughout, i.e. peak D. Overall, the midgut enzyme level with L. donovani infection was 86% of the control value at 30 h post feeding and 105% at 52 h; their relative amounts changed throughout. Soybean trypsin inhibitor enabled L. donovani to survive and multiply in P. papatasi. It is suggested that a specific component of the trypsin-like activity prevents the survival of L. donovani in P. papatasi and that modulation of this factor enables L. major to survive.

Animals

Polycyclic aromatic compounds as phototoxic mosquito larvicides.

The phototoxicity of 2-acetylnaphthalene, 1-acetylnaphthalene, 1-naphthalenecarboxaldehyde, 9-xanthenone, 9-thioxanthenone, 9-methylanthracene, anthracene, alpha-terthienyl, pyrene and fluoranthene was tested with larvae of Aedes aegypti, Ae. taeniorhynchus and Culex quinquefasciatus. The larvae were exposed to the chemicals in the presence of sunlight for intervals from 1 to 6 hr and the corresponding LC50 values calculated. The LC50 values determined when the 6-hr exposure was followed by 18 hr in the dark range from over 10 ppm to below 0.001 ppm. Naphthalene derivatives were the least active while alpha-terthienyl, anthracene, 9-methylanthracene, pyrene and fluoranthene were the most phototoxic.

Animals

On the mechanism of amylose branching by potato Q-enzyme.

1. When potato Q-enzyme converts amylose into an amylopectin-like molecule, the action is by a random, endo-type transglycosylation of the substrate chains. 2. Inter-chain transfer takes place during the formation of the amylopectin branch linkage. This is seen in experiments in which radioactive label was transferred between substrates of disparate molecular weight. Intra-chain transfer, leading to the formation of a branch linkage, is not excluded by these experiments. 3. The minimum length of amylose chain that can act as an acceptor in the transglycosylation reaction, under the experimental conditions described, is greater than 40 glucose units. 4. The requirement of Q-enzyme for substrate chains at least 40 glucose units in length is interpreted as meaning that a stabilized secondary and tertiary structure must be established in the substrate before it can be utilized by Q-enzyme, and that the forces that provide such conformation are sufficiently strong only when the chains are longer than the minimum. Inter-chain transfer is seen as taking place by one of two mechanisms. The first involved the reaction of the enzyme with a chain that has a stabilized (helical?) conformation. An enzyme-donor chain intermediate is formed, that then reacts with an acceptor chain to complete the transglycosylation. The second mechanism envisages the substrate for the enzyme as being a complex formed between two chains (a double helix?). The enzyme encounters the complex and carries out an inter-chain transglycosylation reactions.

1,4-alpha-Glucan Branching Enzyme

Purification and properties of potato 1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-alpha-(1,4-alpha-glucano)-transferase. Evidence against a dual catalytic function in amylose-branching enzyme.

Q-Enzyme, the enzyme that synthesizes the 1,6-alpha-glucosidic branch linkages of amylopectin, has been purified from potato to near homogeneity. The molecular weight of the enzyme is 85000. The active enzyme is a monomer, with a molar activity at pH 7.0 and 24 degrees C of 15. The energy of activation is 25 kJ/mol below 15 degrees C, changing sharply to 63 kJ/mol above that temperature. Enzyme activity is not affected by Mg2+ or ATP. There are about 11 readily titratable sulfhydryl groups per molecule. The evidence that the enzyme is a single protein entity, without hydrolytic activity towards amylose, contrasts with an earlier report that Q-enzyme consists of two components, a hydrolase with molecular weight 70000, and a transferase with molecular weight 20000. Q-enzyme acts on native and synthetic amyloses to give products resembling amylopectin in terms of average unit chain length, degress of beta-amylolysis and iodine stain. The profiles of the unit chains of these synthetic products are, however, different from that of native amylopectin. Additional branch linkages are introduced by Q-enzyme into potato amylopectin, but the product bears no resemblance to phytoglycogen.

1,4-alpha-Glucan Branching Enzyme