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MeSH Review

Cajanus

 
 
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Disease relevance of Cajanus

 

High impact information on Cajanus

  • Glycine max (soybean) and Cajanus cajan (pigeon pea) plants inoculated with the rkpH, rkpG, and rkpH exoA derivatives of S. fredii HH103 showed reduced nodulation and severe symptoms of nitrogen starvation [1].
  • Purification of Cajanus cajan root lectin and its interaction with rhizobial lipopolysaccharide as studied by different spectroscopic techniques [4].
  • The amounts of phenylalanine and hydroxybenzoic acid in a Cajanus cajan methanolic extract were estimated [5].
  • The enzyme urease (urea amidohydrolase, EC 3.5.1.5) prepared from Cajanus indicus, has been immobilized with glutaraldehyde-treated chitin as the solid support [6].
  • We have earlier reported the purification of a non-helical proteinase inhibitor from Cajanus cajan and a helical proteinase/amylase inhibitor from Phaseolus aureus [7].
 

Anatomical context of Cajanus

  • Two classes of mutants, one nonchemotactic towards nutrients (amino acids and sugars) and signal compounds like flavonoids and the other, nonchemotactic towards amino acids and sugars but positive towards naringenin, the flavonoid present in Cajanus cajan root exudate, were obtained [8].
 

Associations of Cajanus with chemical compounds

  • Phenylalanine is the predominant antisickling agent in Cajanus cajan seed extract [9].
  • A methanol extract of the pod surfaces of Cajanus cajan, a feeding stimulant for fifth-instar Helicoverpa armigera, was shown to contain four main phenolic compounds [10].
  • A protein proteinase inhibitor (PI) has been purified from pigeonpea Cajanus cajan (L.) PUSA 33 variety by acetic-acid precipitation, salt fractionation and chromatography on a DEAE-Cellulose column [11].
  • Pigeonpea (Cajanus cajan L) seeds were analysed quantitatively for amylase inhibitor (AI) activity and qualitatively, by an in-gel-detection method on polyacrylamide gels [12].
  • Immobilization of pigeonpea (Cajanus cajan) urease on DEAE-cellulose paper strips for urea estimation [13].
 

Gene context of Cajanus

  • Differential inhibition of Helicoverpa armigera gut proteinases by proteinase inhibitors of pigeonpea (Cajanus cajan) and its wild relatives [14].
  • When serum arginase and ornithine transcarbamylase activities were assayed, it was seen that the group on the unbalanced protein (Cajanus cajan) diet showed less increase on exposure and a tendency to return to normal level earlier than the group on the balanced protein (egg) diet [15].
  • Single Step Immobilized Metal Ion Affinity Precipitation/Chromatography Based Procedures for Purification of Concanavalin A and Cajanus cajan Mannose-Specific Lectin [16].

References

  1. Sinorhizobium fredii HH103 mutants affected in capsular polysaccharide (KPS) are impaired for nodulation with soybean and Cajanus cajan. Parada, M., Vinardell, J.M., Ollero, F.J., Hidalgo, A., Gutiérrez, R., Buendía-Clavería, A.M., Lei, W., Margaret, I., López-Baena, F.J., Gil-Serrano, A.M., Rodríguez-Carvajal, M.A., Moreno, J., Ruiz-Sainz, J.E. Mol. Plant Microbe Interact. (2006) [Pubmed]
  2. Expression of hemagglutinin protein of Rinderpest virus in transgenic pigeon pea [Cajanus cajan (L.) Millsp.] plants. Satyavathi, V.V., Prasad, V., Khandelwal, A., Shaila, M.S., Sita, G.L. Plant Cell Rep. (2003) [Pubmed]
  3. Indole acetic acid production by a Rhizobium species from root nodules of a leguminous shrub, Cajanus cajan. Datta, C., Basu, P.S. Microbiol. Res. (2000) [Pubmed]
  4. Purification of Cajanus cajan root lectin and its interaction with rhizobial lipopolysaccharide as studied by different spectroscopic techniques. Naeem, A., Khan, R.H., Vikram, H., Akif, M. Arch. Biochem. Biophys. (2001) [Pubmed]
  5. Antisickling activity of hydroxybenzoic acids in Cajanus cajan. Akojie, F.O., Fung, L.W. Planta Med. (1992) [Pubmed]
  6. Urease bound to chitin with glutaraldehyde. Iyengar, L., Rao, A.V. Biotechnol. Bioeng. (1979) [Pubmed]
  7. Effect of detergents and hexafluoroisopropanol on the conformation of a non-helical and a helical plant protease inhibitor. Haq, S.K., Khan, R.H. Int. J. Biol. Macromol. (2005) [Pubmed]
  8. Chemotaxis of Rhizobium sp.S2 towards Cajanus cajan root exudate and its major components. Pandya, S., Iyer, P., Gaitonde, V., Parekh, T., Desai, A. Curr. Microbiol. (1999) [Pubmed]
  9. Phenylalanine is the predominant antisickling agent in Cajanus cajan seed extract. Ekeke, G.I., Shode, F.O. Planta Med. (1990) [Pubmed]
  10. Phenolic compounds on the pod-surface of pigeonpea, Cajanus cajan, mediate feeding behavior of Helicoverpa armigera larvae. Green, P.W., Stevenson, P.C., Simmonds, M.S., Sharma, H.C. J. Chem. Ecol. (2003) [Pubmed]
  11. Characterization of a proteinase inhibitor from Cajanus cajan (L.). Haq, S.K., Khan, R.H. J. Protein Chem. (2003) [Pubmed]
  12. Amylase inhibitors of pigeonpea (Cajanus cajan) seeds. Giri, A.P., Kachole, M.S. Phytochemistry (1998) [Pubmed]
  13. Immobilization of pigeonpea (Cajanus cajan) urease on DEAE-cellulose paper strips for urea estimation. Reddy K, R.C., Srivastava, P.K., Dey, P.M., Kayastha, A.M. Biotechnol. Appl. Biochem. (2004) [Pubmed]
  14. Differential inhibition of Helicoverpa armigera gut proteinases by proteinase inhibitors of pigeonpea (Cajanus cajan) and its wild relatives. Chougule, N.P., Hivrale, V.K., Chhabda, P.J., Giri, A.P., Kachole, M.S. Phytochemistry (2003) [Pubmed]
  15. Effect of dietary protein quality on the serum enzymes of rats exposed to simulated hypobaric hypoxic stress. Nikumb, S.K., Santhanam, K., Rao, M.V. Aviation, space, and environmental medicine. (1986) [Pubmed]
  16. Single Step Immobilized Metal Ion Affinity Precipitation/Chromatography Based Procedures for Purification of Concanavalin A and Cajanus cajan Mannose-Specific Lectin. Naeem, A., Khan, R.H., Saleemuddin, M. Biochemistry Mosc. (2006) [Pubmed]
 
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