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
  • 1
    Electronic Resource
    Electronic Resource
    An ATP / ADP γ-phosphate exchange catalyzed by chloroplast ATPase
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Bioenergetics 893 (1987), S. 342-348 
    Details
    ISSN: 0005-2728
    Keywords: (Spinach chloroplast) ; ATP-ADP exchange ; ATPase ; Phosphate exchange ; Photophosphorylation
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0005-2728(87)90055-7
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Thiophosphate analogs of ADP and ATP as substrates in partial reactions of energy conversion in chloroplasts
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Bioenergetics 545 (1979), S. 122-130 
    Details
    ISSN: 0005-2728
    Keywords: (Chloroplast) ; ATPase ; Nucleotide binding ; Photophosphorylation ; Thiophosphate nucleotide analogs
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0005-2728(79)90119-1
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Structure of the active metal-adenosine 5'-triphosphate chelate complex used by light-triggered chloroplast ATPase
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Bioenergetics 809 (1985), S. 117-124 
    Details
    ISSN: 0005-2728
    Keywords: (Spinach chloroplast) ; ATPase ; Coupling factor ; Nucleotide binding ; Phosphorothioate analogue
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0005-2728(85)90174-4
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Loose and tight binding of adenine nucleotides by membrane-associated chloroplast ATPase
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Bioenergetics 723 (1983), S. 71-77 
    Details
    ISSN: 0005-2728
    Keywords: (Spinach chloroplast) ; ATPase ; Adenine nucleotide binding ; Photophosphorylation ; Proton-motive force ; Thylakoid membrane
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0005-2728(83)90010-5
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 5
    Electronic Resource
    Electronic Resource
    Investigations on nucleotide binding sites of isolated chloroplast ATPase by modification with 7-chloro-4-nitrobenzofurazan
    Amsterdam : Elsevier
    FEBS Letters 258 (1989), S. 309-312 
    Details
    ISSN: 0014-5793
    Keywords: ATP-hydrolysis ; ATPase ; Chloroplast ; Covalent modification ; NBD ; Subunit labeling
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0014-5793(89)81681-3
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 6
    Electronic Resource
    Electronic Resource
    Conversion of energy in halobacteria: ATP synthesis and phototaxis (1996)
    Springer
    Archives of microbiology 166 (1996), S. 1-11 
    Details
    ISSN: 1432-072X
    Keywords: Key words Archaea ; Halobacteria ; Energy ; transduction ; Retinal protein ; Proton gradient ; Nitrate ; reductase ; ATPase ; Adaptation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Halobacteria are aerobic chemo-organotroph archaea that grow optimally between pH 8 and 9 using a wide range of carbon sources. These archaea have developed alternative processes of energy provision for conditions of high cell densities and the reduced solubility of molecular oxygen in concentrated brines. The halobacteria can switch to anaerobic metabolism by using an alternative final acceptor in the respiratory chain or by fermentation, or alternatively, they can employ photophosphorylation. Light energy is converted by several retinal-containing membrane proteins that, in addition to generating a proton gradient across the cell membrane, also make phototaxis possible in order to approach optimal light conditions. The structural and functional features of ATP synthesis in archaea are discussed, and similarities to F-ATPases (functional aspects) or vacuolar ATPases (structural aspects) are presented.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002030050349
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 7
    Electronic Resource
    Electronic Resource
    Evolution and ultrastructure of the bovine spermatogonia precursor cell line (1995)
    Springer
    Cell & tissue research 281 (1995), S. 249-259 
    Details
    ISSN: 1432-0878
    Keywords: Key words: Stem cells ; Testis ; PGP 9.5 ; Ultrastructure ; Tubular whole-mounts ; Bovine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. The spermatogonial stem cell line in prepubertal and adult bovine testis was studied by electron microscopy and protein gene product 9.5 immunohistochemistry. Three successive spermatogonia precursor cell configurations were observed. Small basal stem cells were found to possess a spherical shape and nuclei with two to three nucleoli. They were observed in prepubertal testes (25 and 30 weeks) and in low numbers during all the stages of the seminiferous epithelial cycle in the adult. Aggregated spermatogonia precursor cells are the dominating germ cell type in the 25-week-old and 30-week-old calf. In the adult seminiferous epithelium, they cause expansion of the basal tubular compartment as they form dense groups containing up to 15 cells. These groups are observed concomitantly with cycling A-spermatogonia and preleptotenes at the beginning of spermatocytogenesis. At the end of A-spermatogonia propagation, the aggregated spermatogonia precursor cells separate and intermingle with cycling A-spermatogonia. The spermatogonia precursor cells can later be found together with I-spermatogonia as members of an interconnected cellular network of medium-sized cells. When the I-spermatogonia divide to form the smaller B-spermatogonia, the precursor cells, which stay connected with the cycling spermatogonial population, pass through a growth phase. They can now be considered as committed spermatogonia precursor cells and are continuously being transformed into A1-spermatogonia to start a new round of spermatocytogenesis. Ultrastructurally, all members of the precursor cell line are similar. However, a number of features have been found to show a quantitative increase (endoplasmic reticulum, mitochondria) or to exhibit a rising degree of complexity (nucleolus) during the progression from basal stem cells to committed spermatogonia precursor cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00583394
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 8
    Electronic Resource
    Electronic Resource
    Evolution and ultrastructure of the bovine spermatogonia precursor cell line (1995)
    Springer
    Cell & tissue research 281 (1995), S. 249-259 
    Details
    ISSN: 1432-0878
    Keywords: Stem cells ; Testis ; PGP 9.5 ; Ultrastructure ; Tubular ; Whole-mounts ; Bovine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The spermatogonial stem cell line in prepubertal and adult bovine testis was studied by electron microscopy and protein gene product 9.5 immunohistochemistry. Three successive spermatogonia precursor cell configurations were observed. Small basal stem cells were found to possess a spherical shape and nuclei with two to three nucleoli. They were observed in prepubertal testes (25 and 30 weeks) and in low numbers during all the stages of the seminiferous epithelial cycle in the adult. Aggregated spermatogonia precursor cells are the dominating germ cell type in the 25-week-old and 30-week-old calf. In the adult seminiferous epithelium, they cause expansion of the basal tubular compartment as they form dense groups containing up to 15 cells. These groups are observed concomitantly with cycling A-spermatogonia and preleptotenes at the beginning of spermatocytogenesis. At the end of A-spermatogonia propagation, the aggregated spermatogonia precursor cells separate and intermingle with cycling A-spermatogonia. The spermatogonia precursor cells can later be found together with I-spermatogonia as members of an interconnected cellular network of medium-sized cells. When the I-spermatogonia divide to form the smaller B-spermatogonia, the precursor cells, which stay connected with the cycling spermatogonial population, pass through a growth phase. They can now be considered as committed spermatogonia precursor cells and are continuously being transformed into A1-spermatogonia to start a new round of spermatocytogenesis. Ultrastructurally, all members of the precursor cell line are similar. However, a number of features have been found to show a quantitative increase (endoplasmic reticulum, mitochondria) or to exhibit a rising degree of complexity (nucleolus) during the progression from basal stem cells to committed spermatogonia precursor cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00583394
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 9
    Electronic Resource
    Electronic Resource
    Immunohistochemical demonstration of nerve growth factor receptor in bovine testis (1996)
    Springer
    Cell & tissue research 285 (1996), S. 189-197 
    Details
    ISSN: 1432-0878
    Keywords: Key words: Testis ; Nerve growth factor receptor ; Immunohistochemistry ; Ultrastructure ; Bovine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. Nerve growth factor receptor (low-affinity form) was demonstrated immunohistochemically in bovine testis by using a monoclonal mouse anti-human antibody. In the 7-month-old fetus and in the early postnatal testis, the peritubular and intertubular fibroblast-like mesenchymal cells showed a strong reaction. Following differentiation of these cells into Leydig and myoid peritubular cells, the nerve growth factor receptor was no longer expressed. However, peritubular and intertubular testicular fibroblasts/fibrocytes, which are also derived from mesenchymal precursors, remained positive. Additionally, the nerve growth factor receptor was demonstrated in postnatal prespermatogonia, A-spermatogonia, I-spermatogonia and members of the spermatogonia precursor cell line; B-spermatogonia remained negative. In A-spermatogonia and I-spermatogonia, the expression of the nerve growth factor receptor was cell-cycle-dependent and was mostly observed during G1-phase. Pre-embedding ultrahistochemistry with gold-conjugated antibody followed by silver-enhancement revealed that the nerve growth factor receptor was localized at the outer cell surface. The metal granules showed a regular distribution in positive spermatogonia. In testicular fibroblasts/fibrocytes the long narrow processes were preferentially decorated.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004410050636
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 10
    Electronic Resource
    Electronic Resource
    ATP-synthesis in archaea: Structure-function relations of the halobacterial A-ATPase (1998)
    Springer
    Photosynthesis research 57 (1998), S. 335-345 
    Details
    ISSN: 1573-5079
    Keywords: ATPase ; energy transduction ; halobacteria ; Haloferax volcanii ; proton gradient ; subunit structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The archaeal (A)-ATPase has been described as a chimeric energy converter with close relationship to both the vacuolar ATPase class in higher eukaryotes and the coupling factor (F)-ATPase class in eubacteria, mitochondria and chloroplasts. With respect to their structure and some inhibitor responses, A-ATPases are more closely related to the vacuolar ATPase type than to F-ATPase. Their function, ATP synthesis at the expense of an ion gradient, however, is a typical attribute of the F-ATPase class. V-type ATPases serve as generators of a proton gradient driving the accumulation of solutes within vesicles such as the vacuoles of plant cells. The three catalytic subunits (A) of the archaeal ATPases are the largest subunits of the A1-part and, like in V-ATPases, closer related to the F-ATPase β-subunits, whereas B corresponds to F-ATPase α. The catalytic subunits A of archaeal ATPases contain an insert of about 80 amino acids in their primary structures that may be aligned to comparable structures in V-ATPases. The location of this additional peptide in Haloferax volcanii is shown using the 2.8 Å X-ray resolution of the bovine mitochondrial F-ATPase [Abrahams et al. (1994) Nature 370: 621-628]. A three dimensional structure for the catalytic subunit of Haloferax volcanii ATPase is proposed using the Swiss-Model Automated Protein Modelling Server. The halobacterial ATPase is a halophilic protein; it contains about 20% negatively charged amino acid residues. A large portion of acidic residues is located on the outer surface of the protein as well as in the insert of subunit A. This result is discussed in terms of protein stability under high salt stress conditions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006055713117
    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...