NOPR Collection:

H⁺-ATPase as a biochemical marker for early detection of root (wilt) disease in coconut palms (Cocos nucifera L)

2012-12-27T16:31:34Z

Title: H⁺-ATPase as a biochemical marker for early detection of root (wilt) disease in coconut palms (Cocos nucifera L) Authors: Thelly, T Mathews; Mohankumar, C Abstract: H⁺-ATPase activity in leaves and roots of coconut palms growing in 'root wilt disease-prevalent areas' was compared with that of coconut palms growing in 'disease-free areas'. The activity was found to be significantly less in the leaves and roots of palms in the disease-prevalent zone as compared to that in disease-free zone. Histochemical examination of the leaves showed results that corroborated the biochemical findings. The possible application of H⁺-ATPase activity as a marker for the early detection of wilt disease in coconut palms is suggested. Page(s): 199-202

Characterization and biological activities of Chenopodium leaf hemagglutinin (CLH)

2012-12-25T16:32:10Z

Title: Characterization and biological activities of Chenopodium leaf hemagglutinin (CLH) Authors: Suseelan, K N; Sainis, K B; Mitra, R Abstract: A hemagglutinin (CLH) having native molecular mass of 58 kDa and subunit molecular mass of 33 kDa had been purified from thc leaves of Chenopodium amaranticolor. The protein agglutinated rabbit erythrocytes and no agglutination was observed with any of the groups A, B or O of human blood. The amino acid composition revealed that CLH was rich in aspartic acid, glutamic acid, glycine and phenylalanine and also significant amount of methionine. Thc N-terminal amino acid sequence analysis showed that CLH had no homology with any of the plant hcmagglutinins studied so far. It was in active towards human peripheral blood cells but mitogenic for mouse spleen B-Iymphocytes. CLH inhibited protein synthesis in rat thymocytes at high concentration. CLH did not inhibit TMV infection of leaves indicating absence of antiviral properties. Page(s): 193-198

Purification and characterization of a hemagglutinin isolated from the leaves of Chenopodium (Chenopodium amaranticolor)

2012-12-25T16:31:41Z

Title: Purification and characterization of a hemagglutinin isolated from the leaves of Chenopodium (Chenopodium amaranticolor) Authors: Suseelan, K N; Mitra, R Abstract: A hemagglutinin was isolated and purified from the leaves of Chenopodium (Chenopodium amaranticolor) using ionexchange chromatography and affinity chromatography on fetuin- agarose matrix . It agglutinated rabbit erythrocytes. The hemagglutinin had a native molecular mass of 58 kDa, as estimated by gel filtration and showed a single band of molecular mass of 33 kDa on SDS-PAGE. It showed hemagglutinati on activity over the pH range 3-12 and was found to be stable up to 70°C. On isoelectrofocussing, the pl of this hemagglutinin was estimated to be 5.25. However, it was found to contain seven charge variants when isoelectrofocussing was performed in presence of 6M urea. Page(s): 186-192

Purification and characterization of an invertase produced by Aspergillus ochraceus TS

2012-12-25T16:32:07Z

Title: Purification and characterization of an invertase produced by Aspergillus ochraceus TS Authors: Ghosh, Kajari; Dhar, Alok; Samanta, Timir B Abstract: Purification and characterization of an extracellular invertase produced by Aspergillus ochraceus TS are reported. The enzyme was purified (42-fold) from culture filtrate by salt precipitation, ion-exchange and gel filtration. Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) of the purified enzyme showed a single band of molecular mass 66 kDa. The molecular mass of the native enzyme was found to be 130 kDa by gel filtration. The purity of the protein was also checked against its antiserum raised in rabbits by two-dimensional immunodiffusion in agarose gel and Western blot that showed a single band. It is a glycoprotein with mannose as its carbohydrate residue. The enzyme showed high affinity for sucrose with a K_m of 3.5 mM. The amino acid analysis revealed a high proportion of acidic residues but it had a low content of cysteine, histidine and arginine comparable to other fungal invertases. Page(s): 180-185

NOPR Collection:

H+-ATPase as a biochemical marker for early detection of root (wilt) disease in coconut palms (Cocos nucifera L)

Characterization and biological activities of Chenopodium leaf hemagglutinin (CLH)

Purification and characterization of a hemagglutinin isolated from the leaves of Chenopodium (Chenopodium amaranticolor)

Purification and characterization of an invertase produced by Aspergillus ochraceus TS

H⁺-ATPase as a biochemical marker for early detection of root (wilt) disease in coconut palms (Cocos nucifera L)