Withania somnifera (Ashwagandha): A novel source of L-asparaginase

Journal of Integrative Plant Biology

Volumn 51, Issue 2, 2009, Pages 201-206

  Oza, Vishal P ^a   Trivedi, Shraddha D ^a   Parmar, Pritesh P ^a   Subramanian, R B ^a  

^a SARDAR PATEL UNIVERSITY   (India)

Author keywords

Fabaceae; L asparaginase; Purification; Solanaceae; Withania somnifera

Indexed keywords

ASPARAGINASE; VEGETABLE PROTEIN;

AMMONIUM SULFATE; ENZYME ACTIVITY; FILTRATION; MEDICINAL PLANT; PH; PRECIPITATION (CHEMISTRY); PROTEOMICS;

ARTICLE; ENZYMOLOGY; ISOLATION AND PURIFICATION; KINETICS; LEGUME; MEDICINAL PLANT; MOLECULAR WEIGHT; PH; TEMPERATURE; WITHANIA;

ASPARAGINASE; FABACEAE; HYDROGEN-ION CONCENTRATION; KINETICS; MOLECULAR WEIGHT; PLANT PROTEINS; PLANTS, MEDICINAL; TEMPERATURE; WITHANIA;

FABACEAE; MAGNOLIOPHYTA; SOLANACEAE; WITHANIA SOMNIFERA;

EID: 58949100464     PISSN: 16729072     EISSN: 17447909     Source Type: Journal    
DOI: 10.1111/j.1744-7909.2008.00779.x     Document Type: Article

References (28)

1. Blum H, Beyer H, Gross HJ (1987). Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels. Electrophoresis 8, 93-99.
2. Bonthron DT, Jaskolski M (1997). Why a ''benign''mutation kills enzyme activity. Structure-based analysis of the A176V mutant of Saccharomyces cerevisiae L-asparaginase I. Acta Biochim. Pol. 44, 491-504.
3. Borek D, Jaskolski M (2001). Sequence analysis of enzymes with asparaginase activity. Acta Biochim. Pol. 48, 893-902.
4. Cammack K, Marlborough D, Miller D (1972). Physical properties and subunit structure of L-Asparaginase isolated from Erwinia carotovora. Biochem. J. 126, 361.
5. Campbell HA, Mashburn LT, Boyse EA, Old LJ (1967). Two L-asparaginases from Escherichia coli B. Their separation, purification, and antitumor activity. Biochemistry 6, 721-730.
6. DeJong P (1972). L-Asparaginase production by Streptomyces griseus. Appl. Microbiol. 23, 1163.
7. Gallagher MP, Marshall RD, Wilson R (1989). Asparaginase as a drug for treatment of acute lymphoblastic leukemia. Essays Biochem. 24, 1-40.
8. Jones P, Kristiansen T, Einarsson M (1973). Purification and properties of L-asparaginase a from Acinetobacter calcoaeticus. Biochim. Biophys. Acta 327, 146.
9. Kozak M, Jaskolski M (2000). Crystallization and preliminary crystallographic studies of a new crystal form of Escherichia coli L-asparaginase (Ser58Ala mutant). Acta Cryst. D. 56, 509-511.
10. Laemmli U (1970). Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 227, 680-685.
11. Lea PJ, Festenstein GN, Hughes GR, Miflin BJ (1984). An immunological survey of L-asparaginase in seed of Lupinus. Phytochemistry 23, 511-514.
12. Lee B, Yang H (1973). Crystallographic studies on L-Asparaginase from Proteus vulgaris. I. Preliminary crystal data. J. Biol. Chem. 248, 7620.
13. Lineweaver BD (1934). The determination of enzyme constant. J. Am. Chem. Soc. 56, 658.
14. Lough TJ, Reddington BD, Grant MR, Hill DF, Reynolds PHS, Farnden KJF (1992b). The isolation and characterization of a cDNA clone encoding L-asparaginase from developing seeds of Lupin (Lupinus arboreus). Plant Mol. Biol. 19, 391-399.
15. Lowry OH, Rosenbrough NJ, Farr LA, Randal RJ (1951). Protein measurement with the folin phenol reagent. J. Biol. Chem. 193, 265.
16. Lubkowski J, Dauter M, Aghaiypour K, Wlodawer A, Dauter Z (2003). Atomic resolution structure of Erwinia chrysanthemi L-asparaginase. Acta Cryst. D. 59, 84-92.
17. Mathews W, Brown H (1974). Isolation of two L-Asparaginases from Guinea pig liver. Enzyme 17, 276.
18. Mozeena BV, Sivaramakrisnan (1980). Preparation and properties of L-asparaginase from green chillies (Capsicum annum L.). J. Biosci. 2, 291-297.
19. Ortlund E, Lacount MW, Lewinski K, Lebioda L (2000). Reactions of Pseudomonas 7A glutaminase-asparaginase with diazo analogues of glutamine and asparagine result in unexpected covalent inhibitions and suggests an unusual catalytic triad Thr-Tyr-Glu. Biochemistry 39, 1199-1204.
20. Palm GJ, Lubkowski J, Derst C, Schleper S, Rohm KH, Wlodawer A (1996). A covalently bound catalytic intermediate in Escherichia coli asparaginase: Crystal structure of a Thr-89-Val mutant. FEBS Lett. 390, 211-216.
21. Roberts J, Holcenberg J, Dolowy W (1972). Isolation, crystallization and properties of Achromobacteraceae Gulyaminase -Asparaginase with antitumor activity. J. Biol. Chem. 247, 84.
22. Shah CS, Qadry JS (1990). Text Book of Pharmacognosy. B S Shah Prakashan, New Delhi, India.
23. Siechiechowicz K, Ireland R (1989). Isolation and properties of an Asparaginase from leaves of Pisum sativum. Phytochemistry 28, 2275.
24. Sieciechowicz KA, Joy KW, Ireland RJ (1988). The metabolism of asparagine in plants. Phytochemistry 27, 663-671.
25. Soru E, Teodorescu M, Zaharia O, Szabados J, Rudescu K (1972). L-asparaginase from the BCG Strain of Mycobacterium bovis I. purification and in vitro immunosupressive properties. Can. J. Biochem. 50, 1149.
26. Sugimoto H, Odani S, Yamashita S (1998). Cloning and expression of cDNA encoding rat liver 60 KDa lysophospholipase containing an asparaginase-like region and ankyrin repeat. J. Biol. Chem. 273, 12536-12542.
27. Tumbula DL, Becker HD, Chang WZ, Soll D (2000). Domain-specific recruitment of amide amino acids for protein synthesis. Nature 407, 106-110.
28. Whelan H, Wriston J (1974). Purification and properties of L-Asparaginase from Serratia marcescens. Biochim. Biophys. Acta 365, 212.