EXTERNAL AND INTERNAL CARBONIC-ANHYDRASES IN DUNALIELLA SPECIES

被引:33
|
作者
GOYAL, A
SHIRAIWA, Y
HUSIC, HD
TOLBERT, NE
机构
[1] MICHIGAN STATE UNIV,DEPT BIOCHEM,E LANSING,MI 48824
[2] LAFAYETTE COLL,DEPT CHEM,EASTON,PA 18042
[3] NIIGATA UNIV,FAC SCI,DEPT BIOL,NIIGATA 95021,JAPAN
关键词
D O I
10.1007/BF00349158
中图分类号
Q17 [水生生物学];
学科分类号
071004 ;
摘要
Four species of Dunaliella and a carbonic anhydrase deficient mutant of Dunaliella tertiolecta (Butcher), HL 25/8, developed a process for concentrating dissolved inorganic carbon when adapted on air or low CO2 for 24 h in the light. However, the external carbonic anhydrase activities in Dunaliella species were nil or low compared with those in Chlamydomonas reinhardtii (Danegard) or some Chlorella species. D. tertiolecta had low and about equal levels of external and internal carbonic anhydrase. D. parva (Lerche) and the D. tertiolecta mutant had negligible external carbonic anhydrase. D. viridis (Teodoresco) and D. salina (Teodoresco), high salt tolerant species, had high activities of internal carbonic anhydrase but low levels of external carbonic anhydrase. Antiserum prepared against the 37 kDa peptide of extra-cellular carbonic anhydrase from Chlamydomonas reinhardtii was immunoreactive with a polypeptide of 30 kDa in D. tertiolecta and its salt sensitive external carbonic anhydrase (CA) mutant HL 25/8. External CA activity from D. tertiolecta was stimulated about three-fold, by including 0.5 M NaCl in the assay medium, while internal CA was not significantly affected by NaCl. External CA activities in the other species were insensitive to NaCl, while their internal activities were 90% inhibited by 0.5 M NaCl. Sorbitol only partly replaced NaCl in stimulating the external CA from D. tertiolecta. These experiments were performed with Dunaliella spp. grown in controlled laboratory cultures during September through November 1989.
引用
收藏
页码:349 / 355
页数:7
相关论文
共 50 条
  • [1] CARBONIC-ANHYDRASES
    DEUTSCH, HF
    INTERNATIONAL JOURNAL OF BIOCHEMISTRY, 1987, 19 (02): : 101 - 113
  • [2] WHY ARE THERE CARBONIC-ANHYDRASES IN THE LIVER
    DODGSON, SJ
    BIOCHEMISTRY AND CELL BIOLOGY-BIOCHIMIE ET BIOLOGIE CELLULAIRE, 1991, 69 (12): : 761 - 763
  • [3] BOVINE KIDNEY CARBONIC-ANHYDRASES
    GARCON, D
    BARLATIER, A
    LUCCIONI, F
    REYNAUD, J
    COMPTES RENDUS HEBDOMADAIRES DES SEANCES DE L ACADEMIE DES SCIENCES SERIE D, 1975, 281 (22): : 1761 - 1764
  • [4] GENETICS OF THE MAMMALIAN CARBONIC-ANHYDRASES
    TASHIAN, RE
    ADVANCES IN GENETICS, 1992, 30 : 321 - 356
  • [5] STRUCTURE AND FUNCTION OF CARBONIC-ANHYDRASES - IMIDAZOLE BINDING TO HUMAN CARBONIC ANHYDRASE-B AND MECHANISM OF ACTION OF CARBONIC-ANHYDRASES
    KANNAN, KK
    PETEF, M
    FRIDBORG, K
    CIDDRESDNER, H
    LOVGREN, S
    FEBS LETTERS, 1977, 73 (01) : 115 - 119
  • [6] NON-CYTOPLASMIC CARBONIC-ANHYDRASES
    FERNLEY, RT
    TRENDS IN BIOCHEMICAL SCIENCES, 1988, 13 (09) : 356 - 359
  • [7] STRUCTURE AND EXPRESSION OF MAMMALIAN CARBONIC-ANHYDRASES
    EDWARDS, Y
    BIOCHEMICAL SOCIETY TRANSACTIONS, 1990, 18 (02) : 171 - 175
  • [8] HUMAN CARBONIC-ANHYDRASES AND CARBONIC-ANHYDRASE DEFICIENCIES
    SLY, WS
    HU, PY
    ANNUAL REVIEW OF BIOCHEMISTRY, 1995, 64 : 375 - 401
  • [9] CARBONIC-ANHYDRASES FROM HUMAN NEONATAL ERYTHROCYTES
    SELL, JE
    PETERING, HG
    JOURNAL OF LABORATORY AND CLINICAL MEDICINE, 1974, 84 (03): : 369 - 377
  • [10] DIFFERENTIAL INHIBITION OF VARIOUS CARBONIC-ANHYDRASES BY CYANOGEN
    KIRLEY, JW
    DAY, RA
    FEDERATION PROCEEDINGS, 1985, 44 (05) : 1811 - 1811