Biohydrogen Production by Catalytic Supercritical Water Gasification: A Comparative Study.

In this article, supercritical water gasification of biocrude at different conditions was performed and compared to each other. Three scenarios were considered while treating biocrude originating from cattle manure (CM) and corn husk (CH), namely, uncatalyzed feedstock, catalyzed with 10% Ni-0.08% Ru/AlO and finally catalyzed with 10% Ni-0.

Characterization of the highly divergent U2 RNA homolog in the microsporidian Vairimorpha necatrix.

An RNA homologous to U2 RNA and a single copy gene encoding the RNA homolog have been characterized in the microsporidian, Vairimorpha necatrix. The RNA which is 165 nucleotides in length possesses significant similarity to U2 RNA, particularly in the 5' half of the molecule. The U2 homolog contains the highly conserved GUAGUA branch point binding sequence seen in all U2 RNAs except those of the trypanosomes.

Partial purification and properties of a pre-mRNA splicing activity.

Precursor RNA substrates for splicing reaction were synthesized in vitro from a plasmid DNA in which the early region 2 gene of adenovirus 2 was fused to an efficient bacteriophage promoter (Salmonella phage 6). Pre-mRNA splicing activity from nuclear extracts of MOPC-315 mouse myeloma cells was partially purified 108-fold by three chromatographic steps. The in vitro splicing reaction catalyzed by the partially purified fractions was efficient (60-80% substrate conversion) and accurate at the nucleotide level.

Differential membrane protein carboxyl-methylation of intact human erythrocytes by exogenous methyl donors.

The patterns of membrane protein carboxyl-methylation by protein methylase II (S-adenosylmethionine: protein-carboxyl O-methyltransferase, EC 2.1.1.

Alkylation of protein by methyl methanesulfonate and 1-methyl-1-nitrosourea in vitro.

Methylation of horse heart cytochrome c has been examined in vitro with [methyl-14C]methanesulfonate (MMS) and [1-methyl-14C]-1-nitrosourea (MNU) as alkylating agents. Analysis of protein hydrolyzates by an automatic amino acid analyzer indicates that, at pH 9.0 with MMS, epsilon-N-monomethyl-lysine is found to be the only major methylated basic amino acid.

Cytochrome c specific methylase from wheat germ.

The cytochromes c of plants (e.g., wheat germ) possess two trimethyllysines, residues 72 and 86.

Effect of methylation on the stability of cytochrome c of Saccharomyces cerevisiae in vivo.

The in vivo stability of methylated and unmethylated cytochrome c in Saccharomyces cerevisiae was studied by pulse-labeling the hemoproteins with [methyl-3H]-methionine and/or [2-14C]methionine and following the fate of these proteins under anaerobiosis and in the presence of cycloleucine. These two conditions will respectively block further cytochrome c synthesis and inhibit methylation by lowering the cellular S-adenosyl-L-methionine pool and, thus, permit an unambiguous interpretation of the data. The results showed that the rate of degradation of unmethylated cytochrome c was constant throughout the chase period, while methylated cytochrome c degradation was seen only in the later part of cold chase.

Enzymatic trimethylation of residue-72 lysine in cytochrome c. Effect on the total structure.

A highly purified protein methylase III from Neurospora crassa or Saccharomyces cerevisiae specifically methylates a single lysine residue of position 72 of horse heart cytochrome c. The enzymatically methylated cytochrome c has been separated from the unmethylated counterpart species by isoelectric focusing. Simultaneously, the pI values of these two species were found to be 9.