Go toArchive
Browse byFacets
Bookbag ( 0 )
'Saccharomyces cerevisiae' in keywords
Results  3 Items
Sorted by   
Publication Year
1997 (1)
1991 (1)
1983 (1)
1Author    Hans Eckstein, Heike SchlobohmRequires cookie*
 Title    A Particulate Guanylate Cyclase (EC from Growing Yeast Cells {Saccharomyces cerevisiae)  
 Abstract    The detection of cGMP in yeast (Eckstein 1988), but lacking hints at guanylate cyclase from sequencing of the yeast genome, raised questions about existence, isoform, and regula­ tion of guanylate cyclase from this organism. We found a particulate guanylate cyclase activity in yeast extracts, exhibiting properties of an integral membrane protein. Characteristics are: pH-optimum at pH 6.8, temperature-optimum around 60 °C, only slight stimulation by Mn2+. Sigmoidal enzyme kinetics indicate allosteric regulation, ATP and Ca2+ act as negative allo-steric effectors. The enzyme activity is increased by yeast alpha-1 mating factor, and by sodium nitrite, thus showing properties of particulate as well as of soluble isoforms from other eukaryotes. The activation by alpha-1 mating factor suggests receptor functions, and a role in ascospore conjugation. 
  Reference    Z. Naturforsch. 52c, 373—379 (1997); received Decem ber 23 1996/February 11 1997 
  Published    1997 
  Keywords    Guanylate Cyclase, Signal Transduction, cGMP, (Saccharomyces cerevisiae) 
  Similar Items    Find
 TEI-XML for    default:Reihe_C/52/ZNC-1997-52c-0373.pdf 
 Identifier    ZNC-1997-52c-0373 
 Volume    52 
2Author    Z. NaturforschRequires cookie*
 Title    of Saccharomyces cere visiae  
 Abstract    The mating pherom one o f baker's yeast, the a-factor, is a dodeca-/tridecapeptide, which is not antigenic by itself. It was coupled to succinylated thyroglobulin by the car-bodiimide procedure to facilitate selective coupling of the a-factor mainly by its N-terminal region. Antibodies against this conjugate were raised in rabbits. After selective precipitation of the rabbit antiserum with succinylated carrier prior to the radial double diffusion test (Ouchter-lony) specific antibodies against the coupled a-factor could be detected. 
  Reference    Z. Naturforsch. 38c, 1069—1071 (1983); received April 21/Septem ber 5/1983 
  Published    1983 
  Keywords    a-Factor, Antibodies, Pheromone, Saccharomyces cerevisiae 
  Similar Items    Find
 TEI-XML for    default:Reihe_C/38/ZNC-1983-38c-1069_n.pdf 
 Identifier    ZNC-1983-38c-1069_n 
 Volume    38 
3Author    Susana Raquel, Correa Garcia, MariaVictoria Rossetti, Alcira Maria, Carmen Batlle, Porfirinas, Porfirias-C Ip, Y. P., N. Ic, E. T., F.C E, N.Requires cookie*
 Title    Studies on Porphobilinogen-Deaminase from Saccharomyces cerevisiae  
 Abstract    Porphobilinogen-deaminase from Saccharomyces cerevisiae has been isolated and partially purified 80-and 230-fold in the absence or presence o f phenylmethylsulphonyl fluoride, re­ spectively. Some properties o f the isolated enzyme were studied. Porphyrin formation was linear with time and protein concentration. O ptim um pH was about 7.5-7.8. Molecular mass o f the pro­ tein was 30,000 ± 3000 Dalton when the enzyme was purified in the presence o f phenylmethyl­ sulphonyl fluoride. A less active and unstable 20,000 D a molecular mass species was obtained when purification was performed in the absence o f the protease inhibitor. Porphobilinogen-deaminase exhibited classical Michaelis-Menten kinetics. The apparent Ky for uroporphyrinogen formation was 19 hm; Fmax was 3.6 nmol uroporphyrin/h and the Hill coefficient was n = 1. Also the action o f several reagents on the activity was studied. Protective thiol agents had no effect. Heavy metals inhibited both porphyrin formation and porphobilinogen consumption, but known sulphydryl inactivating chemicals inhibit the former without modifying the latter. A m m o nium ions had no effect on the activity while hydroxylamine completely inhibited both porphyrin form ation and porphobilinogen consumption. 
  Reference    Z. Naturforsch. 46c, 1017—1023 (1991); received December 17 1990/May 27 1991 
  Published    1991 
  Keywords    Saccharomyces cerevisiae, Yeast, Porphobilinogen-Deaminase, Porphyrin Biosynthesis, Porphobilinogen 
  Similar Items    Find
 TEI-XML for    default:Reihe_C/46/ZNC-1991-46c-1017.pdf 
 Identifier    ZNC-1991-46c-1017 
 Volume    46