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H Budzikiewicz

Publications and source records attributed to H Budzikiewicz.

At least 73 records · Page 4Linked to original sources
PubMedDate not supplied

Detection and quantitation of amphetamine and methamphetamine: electron impact and chemical ionization with ammonia--comparative investigation on Shimadzu QP 5000 GC-MS system.

Gas chromatographic-mass spectrometric (GC-MS) analyses of amphetamine and methamphetamine with chemical ionization (CI) (NH3) and electron impact (EI) were compared after solid-phase extraction from urine. The optimal CI (NH3) conditions for amphetamines were selected; the CI mass spectra of amphetamine, methamphetamine, methylenedioxyamphetamine (MDA), methylenedioxymethamphetamine (MDMA), and methylenedioxyethylamphetamine (MDEA) were obtained. Amphetamine and methamphetamine were monitored as [M+H]+ ions in SIM mode. Under these conditions the GC-MS limits of detection and quantitation were determined for amphetamine (2.1 and 5.0 mg/L, respectively) and for methamphetamine (0.9 and 2.0 mg/L, respectively). The heptafluorobutanoyl (HFB) derivatives were used to increase the sensitivity of the GC-MS analysis of amphetamines. Under CI (NH3) conditions these compounds form mainly the cluster ions [M+NH4]+. For HFB-derivatives the limits of detection and quantitation for CI (NH3) were 95 and 170 micrograms/L, respectively, for amphetamine (m/z 349) and 90 and 160 micrograms/L, respectively, for methamphetamine (m/z 363). For EI they were 10 and 30 micrograms/L, respectively, for amphetamine (m/z 240) and 9 and 27 micrograms/L, respectively, for methamphetamine (m/z 254). The GC-MS-CI (NH3) technique was found to be suitable for confirmation of amphetamine and methamphetamine in urine samples in addition to the routine GC-MS-EI method.

Amphetamine↗
PubMedDate not supplied

Structure and characterization of isopyoverdin from Pseudomonas putida BTP1 and its relation to the biogenetic pathway leading to pyoverdins.

Pyoverdin type siderophores produced by six fluorescent Pseudomonas strains isolated from different rhizospheres were purified and characterized. The purified ferri-pyoverdins were tested for their ability to promote the growth of other strains grown under iron deficiency conditions. Only the one obtained from Pseudomonas putida BTP1 did not act as a growth promoter. The structure of the BTP1 siderophore was elucidated by spectroscopic methods and degradation studies. It turned out that it contains a chromophore which differs from the one typical for pyoverdins insofar as it carries the carboxyl group in 3- rather than in 1-position ((3S)-5-amino-1,2-dihydro-8,9-dihydroxy-3H-pyrimido[1,2a]quinoline-3- carboxylic acid). The amino group of the chromophore is substituted with the 5-carboxyl group of L-glutamic acid and its carboxyl group with the N-terminus of the peptide L-Asp-L-Ala-L-Asp-D-N5-Ac-N5-OH-Orn-L-Ser-L-c-N5-OH-Orn. This isopyoverdin fits into the biogenetic scheme which postulates ferribactins as the precursors of pyoverdins.

Amino Acid Sequence↗
PubMedDate not supplied

Structure elucidation of azotobactin 87, isolated from Azotobacter vinelandii ATCC 12837.

Chromopeptide siderophores (azotobactin 87-I and -II) were isolated from an iron deficient culture medium of Azotobacter vinelandii ATCC 12837 (= DSM 87). Their structures were elucidated by chemical degradation studies and spectroscopic methods, especially 2D-NMR-techniques. Total assignments of 1H-, 13C-, and 15N-resonances based on 2D-HOHAHA-, 1H/13C-HMQC-, 1H/13C-HMBC-, 1H/15N-HMQC/TOCSY-, and 1H/15N-HMBC-experiments are given as well as sequential information derived from 1H/1H-NOESY-, 1H/13C-HMBC- and 1H/15N-HMBC-experiments. Both Az 87-I and Az 87-II consist of a tetracyclic chromophore-- (1S)8,9-dihydroxy-4-oxo-2,3,4,5-tetrahydro-1H,10cH-3a,5,10b- triazaacephenantrylene-1-carboxylic acid--and a decapeptide chain linked with the N-terminus to the carboxy group of the chromophore containing also modified, non-proteinogenic amino acids. The sequence L-Ser-D-Ser-L-Hse-Gly-D-threo-OHAsp-Hse-Hse-Hse-D-N5OH-N5-R- Hbu-Orn-L-Hse was determined for Az 87-I, while Az 87-II contains a C-terminal L-Hse-lactone instead. Iron is chelated by the catecholic group of the chromophore, the beta-hydroxy aspartic acid, and the hydroxamate function formed by N5-hydroxyornithine and R-beta-hydroxybutyric acid.

Amino Acid Sequence↗
PubMedDate not supplied

Structure elucidation of a purple peptide found during the purification of a recombinant protein from Escherichia coli.

A purple substance (4) partially co-purified with a recombinant human B-type natriuretic peptide (hBNP), following an E. coli fermentation. The structure of the compound was elucidated by NMR, electrospray and FAB mass spectrometry. The chromophore is a 1,4-naphthoquinone condensed with the N-terminal cysteine of a heptapeptide by its NH2- and SH-groups to form a dihydro-thiazine ring. The peptide sequence was determined as Cys-Lys-Val-Leu-Arg-Arg-His by mass spectrometric techniques. CID and data base matching identified it as the C-terminus of the 32-amino-acid recombinant peptide hBNP. This modification of an N-terminal Cys may be a more general phenomenon with implications for the production of heterologous proteins by microorganisms.

Amino Acid Sequence↗
PubMedDate not supplied

A pyoverdin from Pseudomonas sp. CFML 95-275.

From Pseudomonas sp. CFML 95-275 a pyoverdin was isolated with a cyclopeptidic substructure. It could be shown that this pyoverdin is identical with one obtained from Pseudomonas fluorescens BTP 7 for which a lactone structure had been deduced from the interpretation of a FAB spectrum. The elucidation of the correct structure of the pyoverdin is described.

Amino Acid Sequence↗
PubMedDate not supplied

Succinopyoverdins--a new variety of the pyoverdin chromophore.

Pseudomonas spp. of the fluorescent group produce siderophores (so-called pyoverdins) consisting of a peptide chain attached to a pyrimidoquinoline ring system which is derived from a condensation product of L-Dab and D-Tyr. Commonly several related compounds are found to accompany the pyoverdins having the same peptide chain, but differing in the heterocyclic part. The structure elucidation of a new variety (succinopyoverdin) is described here.

Molecular Structure↗