Library

feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    ISSN: 1432-0738
    Keywords: Key words Artificial antigen ; Competitive inhibition enzyme immunoassay ; Sarin ; Detection
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract  Two artificial antigens, N α N ɛ-di(O, O-diisopropyl) phosphoryl L-lysine (DIP)- bovine serum albumin (BSA) conjugate (DIP-BSA) and DIP-KLH (keyhole limpet hemocyanin), were synthesized. Antibodies against sarin (O-isopropyl methylphosphonofluoridate) were obtained after immunization of rabbits with DIP-KLH conjugate. A competitive inhibition enzyme immunoassay (CIEIA) was developed to detect the organophosphorus nerve agent sarin. The antibody solutions could be inhibited by sarin as low as 10-6 mol/l, and the standard curve was linear over 3 orders of magnitude. The coefficients of intraassay and interassay variation of this method were 5.4–6.2% (n=11) and 8.0–9.5% (n=6) at a sarin concentration range of 10-3–10-6 mol/l, respectively. The recovery of sarin in water samples at the concentration of 5×10-5 mol/l was in the range of 96.8–102.5%. The specificity of the antiserum was assessed by comparing the inhibition induced by sarin with soman, Vx, isopropyl alcohol and isopropyl methyl phosphonic acid. The results showed that less than 5 mmol/l soman, 2 mmol/l Vx, 16 mmol/l isopropyl alcohol and 8 mmol/l isopropyl methyl phosphonic acid did not influence the determination of sarin in water samples.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Origins of life and evolution of the biospheres 26 (1996), S. 256-257 
    ISSN: 1573-0875
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Geosciences
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Journal of biological physics 20 (1995), S. 283-287 
    ISSN: 1573-0689
    Keywords: basic element of life chemistry ; model expression ; phosphoryl amino acids ; Origin of life
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Physics
    Notes: Abstract A series of compounds (DAP-AA) composed of an amino acid (AA) and a dialkyl phosphoryl group (DAP) is the basic elements of life chemistry. Self-catalysis of DAP-AA gives the self-assembly oligopeptides, even in aqueous medium at 38°C. The oligo-nucleotides could also be assembled from nucleosides' phosphorylation by DAP-AA. DAP-AA acts as the energy source as well as the phosphoryl donor for the synthesis of nuclic Acids and protein. A general expression for the self assembly system is proposed.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 4
    Electronic Resource
    Electronic Resource
    Springer
    International journal of peptide research and therapeutics 7 (2000), S. 325-329 
    ISSN: 1573-3904
    Keywords: artificial enzyme ; bovine serum albumin ; chemicalprotease ; protein cleavage ; seryl-histidine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract A dipeptide seryl-histidine (Ser-His) was found to have theprotein cleavage activity. BSA was cleaved into smear at aroundpH 5.0–6.0, with a half-life around 15 hr at 60 °C.Phosphate could accelerate the reaction. This is a brand newprotein cleavage system. Since Ser and His are well-knowncatalytic residues at the active sites of many serine proteases,this results might provide clues to the possible roles of shortoligopeptides in the origins of modern enzymes.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 5
    Electronic Resource
    Electronic Resource
    Springer
    International journal of peptide research and therapeutics 7 (2000), S. 325-329 
    ISSN: 1573-3904
    Keywords: artificial enzyme ; bovine serum albumin ; chemical protease ; protein cleavage ; seryl-histidine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary A dipeptide seryl-histidine (Ser-His) was found to have the protein cleavage activity. BSA was cleaved into smear at around pH 5.0–6.0, with a half-life around 15 hr at 60 °C. Phosphate could accelerate the reaction. This is a brand new protein cleavage system. Since Ser and His are well-known catalytic residues at the active sites of many serine proteases, this results might provide clues to the possible roles of short oligopeptides in the origins of modern enzymes.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 6
    ISSN: 0030-493X
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Positive ion fast atom bombardment mass spectrometry of N-diisopropyloxyphosphoryl dipeptides and tripeptides showed a novel cleavage pattern in that only the N-phosphoryl fragment ions gave intense peaks while the C-terminal series of ions was suppressed. The base peak was the N-phosphoryl imino ion responding to the N-terminal residue. These advantages are superior to those of other types of N-protecting groups.
    Additional Material: 3 Tab.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 7
    Electronic Resource
    Electronic Resource
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 27 (1992), S. 746-749 
    ISSN: 0030-493X
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Positive ion fast atom bombardment mass spectrometry (FABMS) of in situ N-phosphorylated oligopeptides showed intense quasi-molecular ions together with the successive alkene loss fragment ions, which afford multiple checks of the unequivocal reality of the relative molecular mass of the tested samples. More interesting, in a novel cleavage pattern only the N-phosphoryl fragment ions gave intense peaks, the C-terminal series ions being suppressed. For each of the N-terminal ions, losses of alkenes also occur to provide multiple checks for the existence of these ions. The FABMS of the in situ N- phosphorylated oligopeptides might provide an easily accessible routine method for peptide sequencing.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 8
    Electronic Resource
    Electronic Resource
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 29 (1994), S. 201-204 
    ISSN: 0030-493X
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The fragmentation patterns of N-phosphoamino acids in negative-ion fast atom bombardment mass spectrometry (FABMS) showed different characteristics to those in positive-ion FABMS. Six typical N-diisopropyloxyphorphorylamino acids all had intense [M - 1]- peaks, and they underwent similar fragmentation pathways. In general, the elimination of one alkene molecule followed by the loss of one molecule of alcohol occurred. They also favoured an N → O rearrangement reaction, followed by fragmentation to (RO)2 PO2- and (RO) (HO)PO2-.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 9
    ISSN: 0030-493X
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The positive ion fast atom bombardment mass spectra of N-di-isopropyloxyphosphoryl (Dipp) and N-dibutyloxyphosphoryl (Dbp) amino acids or amino acid methyl esters are presented; and according to the observation of the metastable ions and the high-resolution accurate mass measurement their fragmentation patterns are postulated. Both types of compounds were found to undergo similar fragmentations to produce (HO)2P(O)N=CH—R + H+, in most cases as the most abundant fragment ion of structural significance. An intrinsical difference between the two types of compounds is that N-Dippamino acids appear to favour the successive losses of two molecules of propylene, while the loss of HCOOH seems to be preferred by the Dbp amino acids. For those compounds containing an extra functional group on the side chain of amino acids such as serine or glutamic acid some other type of fragmentation was observed besides the normal phenomenon.
    Additional Material: 2 Tab.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 10
    ISSN: 0887-6134
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Positive ion fast atom bombardment mass spectrometric sensitivities of seven amino acids and the corresponding di-isopropylphosphorylated derivatives were carefully compared. Results showed that an improvement in sensitivity by factors of 4-29, mostly above 10, were achieved after the derivatization. The chemical noise derived from glycerol matrix was also greatly reduced by this derivatization.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...