ABSTRACT
Poly(tetramethylene succinate-co-tetramethylene adipate) (PBSA) and poly(tetramethylenesuccinate) (PBS) were hydrolyzed experimentally into water-soluble oligomers and monomers by Chromobacterium extracellular lipase. The oligomers were identified by high-performance liquid chromatography-mass spectrometry and 1H-nuclear magnetic resonance, which indicated that a total of 28 oligomer species were liberated from PBSA, and that 13 of them were identical to the hydrolysates from PBS. Moreover, 20 of the species were polyester-based compounds of monomer units, and the other 8 species were small amounts of diurethane compounds. Bis(hydroxybutyl) succinate (BSB) and bis(hydroxybutyl) hexamethylene dicarbamate (BHB) were the typical oligomers and were chemically synthesized. Biodegradability of BSB and BHB was examined for 28 d in the activated sludge, and analysis of the results of this study indicated that the final conversion rate of constituent carbon to carbon dioxide was estimated at 80 mol% for BSB and 10 mol% for BHB. The remaining amount of carbon in the undegraded BHB was 20 mol%. In the presence of BSB, the biodegradability of BHB was increased by about 1.5 times. The suggestion was made that BSB induced a growth of microorganisms and helped BHB degradation. This is consistent with the observation that the biodegradation of BHB in native soil for 60 d reached > 60%.
Subject(s)
Adipates/metabolism , Polyesters/metabolism , Succinates/metabolism , Adipates/chemistry , Biodegradation, Environmental , Chromatography, Gel , Chromatography, High Pressure Liquid , Chromobacterium/enzymology , Lipase/metabolism , Magnetic Resonance Spectroscopy , Mass Spectrometry , Molecular Weight , Polyesters/chemistry , Solubility , Spectroscopy, Fourier Transform Infrared , Succinates/chemistry , Water/chemistryABSTRACT
The nucleotide sequence of a 9240-base pair DNA fragment of the mitochondrial (mt) genome of a squid, Loligo bleekeri, was determined, in which 8 protein and 14 tRNA genes were identified. The gene organization of the mt-genome exhibits a greater resemblance to the gene organization of arthropods and a chiton, Katharina tunicata, than to those of a mussel, Mytilus edulis, and land snails. A cloverleaf-like structure was observed between the genes for subunits 4 and 5 of NADH dehydrogenase (ND4 and -5), which is considered to have originated from histidine tRNA. It is presumed that this structure functions as a transcriptional punctuation signal for the maturation of the ND4 and ND5 mRNAs.
Subject(s)
DNA, Mitochondrial/genetics , Decapodiformes/genetics , Adenosine Triphosphatases/genetics , Amino Acid Sequence , Animals , Arthropods/genetics , Base Composition , Base Sequence , Genes , Molecular Sequence Data , NADH Dehydrogenase/genetics , RNA, Transfer/genetics , Transcription, GeneticABSTRACT
We previously reported the isolation of a cDNA encoding the liver-specific isozyme of rat S-adenosylmethionine synthetase from a lambda gt11 rat liver cDNA library. Using this cDNA as a probe, we have isolated and sequenced cDNA clones for the rat kidney S-adenosylmethionine synthetase (extrahepatic isoenzyme) from a lambda gt11 rat kidney cDNA library. The complete coding sequence of this enzyme mRNA was obtained from two overlapping cDNA clones. The amino acid sequence deduced from the cDNAs indicates that this enzyme contains 395 amino acids and has a molecular mass of 43,715 Da. The predicted amino acid sequence of this protein shares 85% similarity with that of rat liver S-adenosylmethionine synthetase. This result suggests that kidney and liver isoenzymes may have originated from a common ancestral gene. In addition, comparison of known S-adenosylmethionine synthetase sequences among different species also shows that these proteins have a high degree of similarity. The distribution of kidney- and liver-type S-adenosylmethionine synthetase mRNAs in kidney, liver, brain, and testis were examined by RNA blot hybridization analysis with probes specific for the respective mRNAs. A 3.4-kilobase (kb) mRNA species hybridizable with a probe for kidney S-adenosylmethionine synthetase was found in all tissues examined except for liver, while a 3.4-kb mRNA species hybridizable with a probe for liver S-adenosylmethionine synthetase was only present in the liver. The 3.4-kb kidney-type isozyme mRNA showed the same molecular size as the liver-type isozyme mRNA. Thus, kidney- and liver-type S-adenosylmethionine synthetase isozyme mRNAs were expressed in various tissues with different tissue specificities.
Subject(s)
DNA/genetics , Kidney/enzymology , Methionine Adenosyltransferase/genetics , Transferases/genetics , Amino Acid Sequence , Animals , Base Sequence , Blotting, Northern , Cloning, Molecular , DNA Probes , Isoenzymes/genetics , Molecular Sequence Data , RNA/genetics , RNA/isolation & purification , Rats , Sequence Homology, Nucleic AcidABSTRACT
Cytochrome oxidase subunit I gene of a squid (Mollusca), Doryteuthis mitochondrial genome was sequenced. Comparison with the nucleotide sequence and the deduced amino acid sequence of other animal mitochondria suggests that the squid mitochondria has a variation in the genetic code; UGA codes for tryptophan, AUA for methionine and AGA/G for serine. This situation is similar to the case of Drosophila or Ascaris mitochondria.
