Reference

Effects of culture conditions on the growth of Usneaceae lichen tissue cultures

Effects of culture conditions on the growth of Usneaceae lichen tissue cultures. Yamamoto, Yoshikazu; Mizuguchi, Ryuzo; Takayama, Sachiko; Yamada, Yasuyuki (Fac. Agric., Kyoto Univ., Kyoto 606, Japan). Plant Cell Physiol., 28(8), 1421-6 (English) 1987. CODEN: PCPHA5. ISSN: 0032-0781. DOCUMENT TYPE: Journal CA Section: 11 (Plant Biochemistry) Conditions influencing the in vitro growth of tissues from Usneaceae species were investigated. Thallus segments of all species except the alpine lichen grew at 20° on malt-yeast ext. agar medium in the dark. Tissues of the subtropical lichen grew at 29°, but those of other species did not. Cultured U. longissima tissues grew rapidly to about 13 times the initial wt. in 12 wk of culture on Lilly-Barnett medium contg. 2% mannitol. D-Asparagine promoted the growth of cultured lichen tissues, as did the corresponding L-amino acid. Cultured tissues derived from different lichen species used different sugars and amino acids. Addn. of vitamins, phytohormones, and nucleic acid derivs. did not accelerate growth.

Purification and characterization of L-asparaginase with anti-lymphoma activity from Vibrio succinogenes

Purification and characterization of L-asparaginase with anti-lymphoma activity from Vibrio succinogenes. Distasio, John A.; Niederman, Robert A.; Kafkewitz, David; Goodman, David (Dep. Microbiol., Rutgers State Univ., New Brunswick, N. J., USA). J. Biol. Chem., 251(22), 6929-33 (English) 1976. CODEN: JBCHA3. DOCUMENT TYPE: Journal CA Section: 7 (Enzymes) Homogeneous L-asparaginase (EC 3.5.1.1) with antilymphoma activity was prepd. from V. succinogenes, an anaerobic bacterium from the bovine rumen. An overall yield of pure L-asparaginase of 40-45% and a specific activity of 200 IU/mg of protein were obtained. The pure enzyme was stored at -20.degree. for .gtoreq.3 months with no loss of activity. The isoelec. point of the L-asparaginase was 8.74. 2058-58-4 and 1955-68-6 are cas registry numbers of chemicals which are used as reagents here. No carbohydrate, P, tryptophan, or SS or SH groups were detected. The enzyme had a mol. wt. of 146,000 and a subunit mol. wt. of .apprx.37,000. The Km of the enzyme for L-asparagine is 4.78 .times. 10-5 M and the pH optimum of the L-asparaginase reaction was 7.3. D-asparagine was hydrolyzed at 6.5% of the rate found with the L isomer. L-Glutamine and a variety of other amides were not hydrolyzed at significant rates; the activity of the enzyme for L-glutamine was 130- to 600-fold less than that of other therapeutically effective L-asparaginases of bacterial origin. L-asparaginase from V. succinogenes was immunol. distinct from the L-asparaginase (EC-2) of Escherichia coli. .