Library

X
feed icon rss

Your email was sent successfully. Check your inbox.

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

Proceed reservation?

Export
Filter
  • Electronic Resource  (9)
  • 1985-1989  (9)
  • 1988  (9)
  • Nuclear reactions
  • Recombinant DNA
  • Theoretical, Physical and Computational Chemistry
  • 1
    Electronic Resource
    Electronic Resource
    Evaluation of the stability of human erythropoietin in samples for radioimmunoassay (1988)
    Springer
    Journal of molecular medicine 66 (1988), S. 241-245 
    Details
    ISSN: 1432-1440
    Keywords: Erythropoietin ; Stability ; Radioimmunoassay ; Polycythemic mouse bioassay ; Recombinant DNA
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Radioimmunoassays for erythropoietin are limited so far to a few specialized laboratories and this requires transport and storage of samples. We therefore tested the stability of immunoreactive erythropoietin in serum and plasma samples obtained from a uremic and a nonuremic anemic patient. No significant change in the concentration of immunoreactive erythropoietin was found in either serum or plasma samples for up to 14 days of storage. This type of stability was observed no matter whether the samples were stored at room temperature, 4° C, or −20° C. There was no difference between the estimates of erythropoietin in serum and heparinized plasma. Validity of the radioimmunoassay used in this study was demonstrated by parallelism of dilution curves of test specimens and the 2nd International Reference Preparation for erythropoietin and by a close correlation between the immunoreactivity and the bioactivity of the hormone, as assessed in the same samples by the exhypoxic polycythemic mouse bioassay. In conclusion the data obtained clearly indicate that the necessity of storage and transport of clinical samples does not limit the practicability of the radioimmunoassay for erythropoietin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01748163
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Human cytomegalovirus DNA in the temporal cortex of a schizophrenic patient (1988)
    Springer
    European archives of psychiatry and clinical neuroscience 238 (1988), S. 110-113 
    Details
    ISSN: 1433-8491
    Keywords: Schizophrenia ; Cytomegaloviruses ; Virus diseases ; Recombinant DNA
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Using highly sensitive nucleic acids hybridization techniques, which allow the detection of 0.1–0.5 single copy gene equivalents per cell, DNA from the temporal cortex of seven definite schizophrenics, five persons with schizophrenia-like psychoses, three patients with Huntington's chorea and nine mentally normal individuals were probed with human cytomegalovirus (HCMV) DNA. A clear hybridization signal was obtained with DNA from the temporal lobe of a young schizophrenic patient, whereas DNA from the temporal cortex of controls did not hybridize to the HCMV probe. This finding is in agreement with the cytomegalovirus hypothesis of schizophrenia and hints at the possibility that viral infection of the temporal cortex may in some sporadic cases be a contributing factor to the development of schizophrenic psychoses. There is no indication, however, that infection of the central nervous system with HCMV is an aetiological factor in the great majority of schizophrenic disorders. Clearly further studies, preferably in situ hybridizations of whole brains, are needed to prove or disprove the cytomegalovirus hypothesis of schizophrenia.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00452786
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Cloning and nucleotide sequence of the Salmonella typhimurium LT2 metF gene and its homology with the corresponding sequence of Escherichia coli (1988)
    Springer
    Molecular genetics and genomics 212 (1988), S. 246-251 
    Details
    ISSN: 1617-4623
    Keywords: metF ; 5,10-methylenetetrahydrofolate reductase ; Recombinant DNA ; Nucleotide sequence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The Salmonella typhimurium LT2 metF gene, encoding 5,10-methylenetetrahydrofolate reductase, has been cloned. Strains with multicopy plasmids carrying the metF gene overproduce the enzyme 44-fold. The nucleotide sequence of the metF gene was determined, and an open reading frame of 888 nucleotides was identified. The polypeptide deduced from the DNA sequence contains 296 amino acids and has a molecular weight of 33 135 daltons. Mung bean nuclease mapping experiments located the transcription start point and possible transcription termination region for the gene. There is a 25bp nucleotide sequence between the translation termination site and the possible transcription termination region. This region possesses a GC-rich sequence that could form a stable stem and loop structure once transcribed (ΔG=-9 kcal/mol), followed by an AT-rich sequence, both of which are characteristic of rho-independent transcription terminators. The nucleotide and deduced amino acid sequences of the S. typhimurium metF gene are compared with the corresponding sequences of the Escherichia coli metF gene. The nucleotide sequences show 85% homology. Most of the nucleotide differences found do not alter the amino acid sequences, which show 95% homology. The results also show that a change has occurred in the metF region of the S. typhimurium chromosome as compared to the E. coli chromosome.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00334692
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    The repressor gene (c) of the Streptomyces temperate phage ϕc31: Nucleotide sequence, analysis and functional cloning (1988)
    Springer
    Molecular genetics and genomics 213 (1988), S. 269-277 
    Details
    ISSN: 1617-4623
    Keywords: Recombinant DNA ; Helix-turn-helix motifs ; In vitro transcription-translation ; Phage immunity ; Exonuclease III deletions
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The nucleotide sequence of the 3.4 kb SphI-G fragment that contained the repressor gene (c) of the temperate Streptomyces phage ϕc31 was determined. Analysis of this sequence revealed a large open reading frame with protein coding character and sequence changes in c gene point and deletion mutants identified this as the coding region of the repressor. Two of the mutants studied had undergone deletions of 1.1 kb and 1.4 kb that had occurred across short direct repeats of 6 bp and 11 bp, respectively. Coupled in vitro transcription-translation experiments using the cloned SphI-G fragment and Streptomyces lividans cell free extracts identified a protein product of approximately 72 kDa, in close agreement with that predicted from the nucleotide sequence. A strongly predicted helix-turn-helix motif that may be involved in DNA binding occurred towards the carboxy-terminus of the amino acid sequence. Initial attempts to clone the SphI-G fragment in Streptomyces failed; using information gained from the sequence analysis a smaller segment of this DNA fragment was cloned in S. lividans and conferred immunity to a clear plaque mutant (c1) of ϕc31.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00339591
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 5
    Electronic Resource
    Electronic Resource
    A multigene family in Calothrix sp. PCC 7601 encodes phycocyanin, the major component of the cyanobacterial light-harvesting antenna (1988)
    Springer
    Molecular genetics and genomics 211 (1988), S. 296-304 
    Details
    ISSN: 1617-4623
    Keywords: Complementary chromatic adaptation ; Gene expression ; Photoregulation ; Phycobilisome ; Recombinant DNA
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary In cyanobacteria, light is harvested by phycobilisomes which are essentially made up of chromophoric proteins called phycobiliproteins. We have characterized two gene clusters (cpcB1, cpcA1 and cpcB3, cpcA3) each encoding the two subunits of phycocyanin (βPC and αPC, respectively), one of the major phycobiliproteins in Calothrix 7601. Downstream from the gene encoding the PCα subunit in cluster 1, an open reading frame was found, cpcE1. These genes are organized in two transcriptional units, namely: cpcB3 A3 and cpcB1 A1 E1. All these genes are transcribed whatever the chromatic light received during cell growth. Consequently, although only one type of “constitutive” PC has been biochemically characterized, we have demonstrated that there are two cpc operons “constitutively” transcribed in this strain. With the previously described red light “inducible” cpcB2 A2 operon, there are three copies of the PC encoding genes in Calothrix 7601. The significance of this newly described multigene family in cyanobacteria is discussed. We have also mapped the 5′ and 3′ termini of the major transcript from the cpc1 operon. Analysis of the 5′ untranslated region of this transcript has revealed alternative secondary structures which are proposed to play a role in the regulation of the expression of this operon.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00330607
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 6
    Electronic Resource
    Electronic Resource
    Secretion and export of IGF-1 in Escherichia coli strain JM101 (1988)
    Springer
    Molecular genetics and genomics 215 (1988), S. 19-25 
    Details
    ISSN: 1617-4623
    Keywords: IGF-1 ; Escherichia coli secretion/export ; LamB leader peptide ; Heterologous gene expression ; Recombinant DNA
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The processing of LamB-IGF-1 fusion protein and the export of processed IGF-1 (insulin-like growth-factor-1) into the growth medium was examined in the Escherichia coli host strain, JM101. Several strain or plasmid modifications were tried to increase export of periplasmic (Processed) IGF-1 into the growth medium of JM101. These included: (1) use of a lon null mutant strain to increase accumulation levels of unprocessed LamB-IGF-1 fusion protein; (2) use of an alternative drug resistance marker on the expression plasmid rather than beta-lactamase, thereby reducing any competition for processing of LamB-IGF-1 by signal peptidase; (3) examination of whether phage M13 gene III protein expression caused more periplasmic IGF-1 to be exported into the growth medium due to increased outer membrane permeability; and (4) examination of the effect of E. coli or yeast optimized IGF-1 codons. None of these strain or plasmid modifications caused any significant increase in export of IGF-1 into the growth medium of JM101. Solubility studies of LamB-IGF-1 and processed IGF-1 showed that virtually all of the LamB-IGF-1 and IGF-1 remaining within the cell after a 2 h induction period was insoluble. This implied that only soluble LamB-IGF-1 was processed to IGF-1 and that only soluble IGF-1 was exported into the growth medium. Taken together, the results indicated that LamB-IGF-1 and IGF-1 solubility were the limiting factors in secretion of IGF-1 into the periplasm and export of IGF-1 into the growth medium.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00331297
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 7
    Electronic Resource
    Electronic Resource
    Characterization of genetic transformation in Streptococcus oralis NCTC 11427: Expression of the pneumococcal amidase in S. oralis using a new shuttle vector (1988)
    Springer
    Molecular genetics and genomics 215 (1988), S. 53-57 
    Details
    ISSN: 1617-4623
    Keywords: Competence ; Autolysins ; Choline ; Recombinant DNA
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary We have worked out conditions for the study of competence development and genetic transformation in Streptococcus oralis NCTC 11427 (type strain), a species that contains choline in the cell wall. The peak of competence was found at the early exponential phase of growth and the optimal conditions for transformation were achieved with shuttle plasmids prepared from S. pneumoniae or from Escherichia coli serving as donor DNA. Transformation with dye-bouyant density gradient purified plasmid preparations followed first-order kinetics. The pneumococcal amidase can be expressed in S. oralis harbouring a plasmid carrying the lytA gene. This enzyme lysed the cell wall of the transformed cell in the presence of detergents.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00331302
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 8
    Electronic Resource
    Electronic Resource
    Cloning, sequencing and expression of a Bacillus bacteriolytic enzyme in Escherichia coli (1988)
    Springer
    Molecular genetics and genomics 214 (1988), S. 241-248 
    Details
    ISSN: 1617-4623
    Keywords: Autolysin ; Hydrolase ; In vitro transcription and translation ; Recombinant DNA ; Transcriptional and translational signals
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Several hundred bacterial isolates were screened for bacteriolytic activity by growing them on agar medium containing autoclaved, lyophilized Micrococcus lysodeikticus cells as the substrate. A Bacillus sp. producing the largest lytic zone was selected. A genomic bank of this selected bacterium was constructed in the multi-functional vector pTZ18R, with partial SauIIIA DNA fragments inserted at the SalI restriction site. Screening of 800 colonies of this bank for cell lysis gave 5 recombinants exhibiting lytic activity, as detected by analysis of extracts of sonicated Escherichia coli cells on denaturing polyacrylamide gels containing autoclaved, lyophilized M. lysodeikticus cells as the substrate. One clone (pBH2500), expressed inE. coli strain NM522, was found to code for a lytic enzyme corresponding, in molecular weight, to the 27 kDa Bacillus sp hydrolase. This clone with an insertion of 2.5 kb was then subcloned as a 929 bp EcoRI-SauIIIA fragment in pTZ18R (pBH929) and showed higher cell lytic activity. A unique open reading frame for a protein of 251 amino acids, followed by a putative terminator sequence, was found after a consensus ribosome binding site. A putative leader sequence was identified in the first 37 amino acids. One truncated subclone (pBH703), corresponding to 196 out of 251 residues from the protein N-terminal end, still possessed lytic activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00337717
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 9
    Electronic Resource
    Electronic Resource
    Cloning of two chloramphenicol acetyltransferase genes from Clostridium butyricum and their expression in Escherichia coli and Bacillus subtilis (1988)
    Springer
    Molecular genetics and genomics 214 (1988), S. 328-332 
    Details
    ISSN: 1617-4623
    Keywords: Recombinant DNA ; Chloramphenicol resistance ; cat gene ; Plasmids pC194 and pUB110 ; Inducible gene expression
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Two non-homologous chloramphenicol (Cm) acetyltransferase (CAT) genes, designated catA and catB, were cloned from Clostridium butyricum type strains and characterized by restriction mapping. Both genes are efficiently expressed in Escherichia coli and Bacillus subtilis. In contrast to analogous genes from staphylococci and bacilli, gene expression is not dependent on induction by Cm. The genes are considered as chromosomal, since no association with endogenous plasmids was detectable. Southern hybridization revealed a homology between catA and the staphylococcal Cm resistance plasmid, pC194. The subunit size of the clostridial CAT enzymes expressed in E. coli was determined as 22.5 kDa (catA) and 24 kDa (catB), respectively. The C. butyricum cat genes provide potentially useful selection markers for the construction of cloning vectors from cryptic clostridial plasmids.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00337731
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...