Saccharomyces cerevisiae molecular weight

Using gel filtration on columns of Sephadex G-200, Gascon and Ot-tolenghi142 discovered in Saccharomyces cerevisiae a form of /3-D-fruc-tofuranosidase of low molecular weight, and predicted correctly that this form would be found to be free from carbohydrate. This enzyme occurred within the protoplast its molecular weight (135,000) and specific activity were similar to those of the protein moiety of the external enzyme. The two /3-D-fructofuranosidases gave the same Km for sucrose, the same Km for raffinose, and the same pH optimum (3.5 to 5.5) for enzymic activity but their pH-stability curves differed, the internal enzyme being reversibly inactivated under acidic conditions, that is, below pH 5. 

Pmrl (for plasma-membrane ATPase-related) of Saccharomyces cerevisiae was the first intracellular Ca2+-ATPase that was identified as a member of the SPCA family (Rudolph et al., 1989 Antebi and Fink, 1992 Sorin et al 1997). There are no introns in the coding region, like for most genes in S. cerevisiae. The Pmrl protein (GenBank accession no. AAA34884) comprises of 950 amino acids and has a molecular weight of 104 kDa. 

Willsky, G.R., D.A. White, and B.C. McCabe. 1984. Metabolism of added orthovanadate to vanadyl and high-molecular-weight vanadates by Saccharomyces cerevisiae. J. Biol. Chem. 259 13273-81. 

Molecular Weight. Detailed information on the molecular weights of pepsin from several species, chymosin, and fungal enzymes is given by Fruton (46) and Matsubara and Feder (29), They are in the range of 30,000-40,000 for the mammalian gastric proteins and microbial enzymes. A protease from Saccharomyces cerevisiae with a molecular weight of... 

Wang S, Tabernero L, Zhang M et al (2000) Crystal structures of a low-molecular weight protein tyrosine phosphatase firom Saccharomyces cerevisiae and its complex with the substrate p-nitrophenyl phosphate. Biochemistry 39 1903-1914... 

Cytochrome b2 (EC 1.1.2.3) is a tetrameric protein in which each subunit contains one molecule of flavin mononucleotide and one molecule of heme. The molecular weight is 238 000. The enzyme is contained in Saccharomyces cerevisiae and Hansenula anomala, where it transfers electrons in the respiratory chain from lactate to cytochrome c. With the artificial electron acceptor hexacyanoferrateflll) the respective Km values are 0.4 and 1.3 mmol/1. The pH optimum is between 6.5 and 8. 

The gel contains becaplermin, a recombinant human platelet-derived growth factor for topical administration. Becaplermin is produced by recombinant DNA technology by insertion of the gene for the B chain of platelet-derived growth factor into the yeast Saccharomyces cerevisiae. Becaplermin has a molecular weight of approximately 25 kDa and is a homodimer composed of two identical polypeptide chains that are bound together by disulfide... 

Mannan was discovered in bakers yeast (Saccharomyces cerevisiae) by Salkowski in 1894 at that time, it was termed yeast gum. The first detailed studies of its structure were made by the methyl-ation procedure by Haworth and coworkers. - The results showed that the polysaccharide consists entirely of D-mannose residues and is highly branched, the D-mannose residues being combined by (1 2)-, (1 3)-, and (1 — 6)-linkages. Its molecular weight, as... 

In contrast the enzyme purified from lupin root nodule cytosol is reported to consist of a single polypeptide chain of molecular weight 235,000 (Boland and Benny, 1977). No information is available at present regarding the possible subunit structure of other eukaryote glutamate synthases although the ferredoxin-dependent enzyme from V. faba has a molecular weight of 150,000, as determined by gel filtration (Wallsgrove et al., 1977) and the pyridine nucleotide-dependent enzyme of Saccharomyces cerevisiae has a sedimentation coefficient of 14.6 S (Roon et al., 1974). 

Figure 5.9 shows a snapshot of an LC CID MS/MS analysis of a tryptic digest of a standard six-protein mixture. The top mass spectrum (scan 1345 in this experiment) is an FT-ICR survey scan. In the subsequent scan ( 1346), CID MS/MS of the precursor ion m/z 524.9 is performed in the linear ion trap. That precursor ion is the most abundant ion in the survey scan that has not been subjected previously to MS/MS, that is, is not on the exclusion list. Scan 1347 is the CID mass spectrum of precursor mJz 6253, the second most abundant ion, not on the exclusion list, in the survey scan. The sequence ends with CID of precursor m/z 707.6, the third most abundant ion, not on the exclusion list, in the survey scan. The subsequent scan (not shown) is an FT-ICR survey scan. An alternative workflow favored by some researchers is one FT-ICR survey MS scan followed by CID in the linear ion trap of the 10 most-abundant ions [107]. These parallel-processing approaches have been applied to a diverse range of studies including analysis of the chicken egg white proteome [108], the low molecular weight proteome of Halobacterium salinarum [109], the endocervical mucas proteome [110], sumoylation in Saccharomyces cerevisiae [111], and the tear fluid proteome [112]. 

The extracellular enzymes of yeast are glycoproteins and include invertase and acid phosphatase. Strains of Saccharomyces carlsbergensis but not S, cerevisiae also possess melibiase. Yeast invertase has a minimum molecular weight of 27 000 contains 50 % mannan and 2-3 % glucosamine [43]. The precise location of the extracellular enzymes is still uncertain. They may occupy the space (periplasm) between the membrane and the bulk of the wall components, be anchored to the membrane via protein or covalently associated with other mannan or even glucan molecules. 

The original molecular weight assignments (24) for the enzymes from B. subtilis were probably incorrect the ornithine transcarbamylase has now been shown to be a trimer of M, 140,000 and the corresponding enzymes from Saccharomyces cerevisiae which interact in a similar manner, to be discussed below, are both trimers with about the same molecular weight 26). 

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