![]() 赖氨酸-特异性蛋白酶结构式
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常用名 | 赖氨酸-特异性蛋白酶 | 英文名 | Native Achromobacter lyticus Achromopeptidase |
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CAS号 | 123175-82-6 | 分子量 | N/A | |
密度 | N/A | 沸点 | N/A | |
分子式 | N/A | 熔点 | N/A | |
MSDS | 中文版 美版 | 闪点 | N/A | |
符号 |
![]() GHS08 |
信号词 | Danger |
Probing PrPSc structure using chemical cross-linking and mass spectrometry: evidence of the proximity of Gly90 amino termini in the PrP 27-30 aggregate.
Biochemistry 44(30) , 10100-9, (2005) Elucidation of the structure of PrP(Sc) continues to be one of the most important and difficult challenges in prion research. This task, essential for gaining an understanding of the basis of prion infectivity, has been hampered by the insoluble, aggregated n... |
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Analysis of the peptidoglycan hydrolase complement of Lactobacillus casei and characterization of the major γ-D-glutamyl-L-lysyl-endopeptidase.
PLoS ONE 7(2) , e32301, (2012) Peptidoglycan (PG) is the major component of Gram positive bacteria cell wall and is essential for bacterial integrity and shape. Bacteria synthesize PG hydrolases (PGHs) which are able to cleave bonds in their own PG and play major roles in PG remodelling re... |
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Identification of the epsilon-(gamma-glutamyl)lysine cross-linking sites in alpha-lactalbumin polymerized by mammalian and microbial transglutaminases.
J. Agric. Food Chem. 50(25) , 7412-9, (2002) To investigate the site specificity of two transglutaminases (TGases), that is, the enzymes from guinea pig liver (GTGase) and Streptoverticillium (MTGase), the acyl acceptor and donor sites in alpha-lactalbumin were determined. Alpha-lactalbumin was cross-li... |
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An improved protocol for quantification of freshwater Actinobacteria by fluorescence in situ hybridization.
Appl. Environ. Microbiol. 69(5) , 2928-35, (2003) We tested a previously described protocol for fluorescence in situ hybridization of marine bacterioplankton with horseradish peroxidase-labeled rRNA-targeted oligonucleotide probes and catalyzed reporter deposition (CARD-FISH) in plankton samples from differe... |
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The primary structure and structural characteristics of Achromobacter lyticus protease I, a lysine-specific serine protease.
J. Biol. Chem. 264(7) , 3832-9, (1989) The complete amino acid sequence of Achromobacter lyticus protease I (EC 3.4.21.50), which specifically hydrolyzes lysyl peptide bonds, has been established. This has been achieved by sequence analysis of the reduced and S-carboxymethylated protease and of pe... |
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Purification and characterization of perchloric acid soluble protein from rat lung.
Comp. Biochem. Physiol. B Biochem. Mol. Biol. 135(2) , 255-62, (2003) We isolated a perchloric acid soluble protein from the post-mitochondria supernatant fraction of the rat lung and designated it as RLu-PSP1. The protein is soluble in 5% perchloric acid and was purified by ammonium sulfate fractionation and CM-Sephadex chroma... |
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Lytic enzyme, labiase for a broad range of Gram-positive bacteria and its application to analyze functional DNA/RNA.
J. Microbiol. Methods 61 , 251-260 , (2005) The lytic activity of labiase and achromopeptidase for bacterial DNA/RNA extraction were compared. Rapid lysis of many bacterial strains was observed with labiase followed by SDS treatment. Both labiase and achromopeptidase showed high lytic activity against ... |
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A second lysine-specific serine protease from Lysobacter sp. strain IB-9374.
J. Bacteriol. 186(15) , 5093-100, (2004) A second lysyl endopeptidase gene (lepB) was found immediately upstream of the previously isolated lepA gene encoding a highly active lysyl endopeptidase in Lysobacter genomic DNA. The lepB gene consists of 2,034 nucleotides coding for a protein of 678 amino ... |
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Identification of nucleotide binding sites in V-type Na+-ATPase from Enterococcus hirae.
Biosci. Biotechnol. Biochem. 68(2) , 293-9, (2004) A and B subunits of the V-type Na+-ATPase from Enterococcus hirae were suggested to possess nucleotide binding sites (Murata, T. et al., J. Biochem., 132, 789-794 (2002)), although the B subunit did not have the consensus sequence for nucleotide binding. To f... |
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Possible structure and function of the extra C-terminal sequence of pyruvate kinase from Bacillus stearothermophilus.
J. Biochem. 136(4) , 471-6, (2004) The pyruvate kinases from Genus Bacillus and a few other bacteria have an extra C-terminal sequence with a phosphoenolpyruvate binding motif composed of about 110 amino acids. To elucidate the possible structure and function of this sequence, the enzyme lacki... |