GLORIA

GEOMAR Library Ocean Research Information Access

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
    A specific subunit of vitellogenin that mediates receptor binding (1984)
    s.l. : American Chemical Society
    Biochemistry 23 (1984), S. 5774-5780 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00319a016
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Alteration of meiotic chromosomal pairing and synaptonemal complexes by cycloheximide (1971)
    Springer
    Chromosoma 35 (1971), S. 9-27 
    Details
    ISSN: 1432-0886
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract When cells are exposed to cycloheximide during the synaptic period of meiotic prophase, the structure of the synaptonemal complex is markedly altered. The bulk of the lateral component is removed. When lily zygotene microsporocytes are subsequently transferred into a culture medium free from cycloheximide, normal synaptonemal complexes are again seen. Modification of the structure of the synaptonemal complex by treatment with cycloheximide for 4 days has little permanent effect on meiosis except at late zygonema or early pachynema. Treatment at this time produces meiocytes in which no synaptonemal complexes reform. When these cells proceed into diplotene and diakinesis they are devoid of chiasmatic chromosomes. The data suggest that the synaptonemal complex is essential if chiasmata are to be formed, and that a unique period exists when the formation can be interrupted.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00344680
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Pachytene synaptonemal complexes and meiotic achiasmatic chromosomes (1971)
    Springer
    Chromosoma 33 (1971), S. 129-145 
    Details
    ISSN: 1432-0886
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Microsporocytes sometimes undergo an achiasmatic meiosis when placed into culture early in the season at a time after premeiotic “S” but prior to leptonema. Trillium meiocytes were examined by light and electron microscopy to analyze the frequency of cells in various stages of meiotic prophase and the occurrence of the synaptonemal complex at different times of culture. On the basis of the results, a hypothesis is proposed that suggests there is a tripartite sensitive period that occurs between “S” phase and leptonema. Where the cells are in this sensitive period at the time of transplantation into culture determines whether the cells do not enter meiotic prophase, enter but produce achiasmatic division figures, or enter and develop normally.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00285629
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Changes in the synaptinemal complex during meiotic prophase in mosquito oocytes (1966)
    Springer
    Protoplasma 61 (1966), S. 346-386 
    Details
    ISSN: 1615-6102
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01248989
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 5
    Electronic Resource
    Electronic Resource
    Interaction of very low density lipoprotein with chicken oocyte membranes (1985)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 28 (1985), S. 281-288 
    Details
    ISSN: 0730-2312
    Keywords: very low density lipoprotein ; hen ; oocyte membranes ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The interaction of hen 125I-VLDL (very low density lipoprotein) with chicken oocyte membranes was characterized using a rapid sedimentation assay. Equilibrium and kinetic studies showed an apparent dissociation constant (Kd) 8.7-9.1 × 10-8 M or 43.5-45.5 μg VLDL protein/ml. Binding capacity was 2.0 μg VLDL protein/mg membrane homogenate protein. The apparent rate constants were, k1 = 2.4 × l05 M-1min-1 and k2 = 2.1 × 10-2 min-1. Specific binding required the presence of divalent cations. Whereas binding was completely re-stored after treatment with EDTA by the addition of Mn++, only 60% of binding was restored using Ca++.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240280406
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 6
    Electronic Resource
    Electronic Resource
    Protein transport: A selective membrane mechanism (1976)
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 4 (1976), S. 527-548 
    Details
    ISSN: 0091-7419
    Keywords: Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Proteins are selectively sequestered by a number of cell types. However, only in oocytes is the process sufficiently aggravated and specific to be readily studied. In these cells certain serum proteins are taken up in proportions different from those found in the serum.In vitro incubations of hormonally stimulated and synchronous mosquito oocytes show that the only protein capable of initiating the transport process is the female specific yolk protein. Heterologous proteins such as IgG, bovine serum albumin, cytochrome C, and ferritin are inactive. The female specific protein is a phosphoglycolipoprotein. It is synthesized in the fat body, a liver analog in the insect, and passed into the serum before being transported into the oocytes. Preliminary kinetic analysis shows the uptake process to be specific with an apparent Km of about 10-7 M. Glycolytic inhibitors stop protein uptake.The receptor-mediated binding steps in the transport process are most easily studied in the chicken because of the enormous amount of oocyte membrane available from a given oocyte and because up to 1 gm of protein is normally transported per day per oocyte. IgG and the hen specific phosvitin lipovitellin are two of the physiologically important proteins that are transported intact into the chicken oocytes. The uptake appears selective as shown by studies with iodinated proteins. Ferritin conjugated to IgG is shown by electron microscopy to bind to isolated plasma membranes only where coated pits have formed, whereas ferritin alone is not seen localized on any membrane surface. These very specialized regions of the membrane are similar to micropinocytotic pits but, in addition, possess on their cytoplasmic side dense ridges that form the coat. Transport involves binding to the coated pits, the pinching off of the pits, and the subsequent movement of the coated vesicles in the cytoplasm.
    Additional Material: 16 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jss.400040413
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 7
    Electronic Resource
    Electronic Resource
    Influence of buffer ions and divalent cations on coated vesicle disassembly and reassembly (1979)
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 11 (1979), S. 237-250 
    Details
    ISSN: 0091-7419
    Keywords: coated vesicles ; coat dissembly ; coat reassembly ; coat dissociation ; clathrin ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Disruption of the coat of coated vesicles is accompanied by the release of clathrin and other proteins in soluble form. The ability of solubilized coated vesicle proteins to reassemble into empty coats is influenced by Mg2+, Tris ion concentration, pH, and ionic strength. The proteins solubilized by 2 M urea spontaneously reassemble into empty coats following dialysis into isolation buffer (0.1 M MES-1 mM EGTA-1 mM MgCl2-0.02% NaN3, pH 6.8). Such reassembled coats have sedimentation properties similar to untreated coated vesicles. Clathrin is the predominant protein of reassembled coats; most of the other proteins present in native coated vesicles are absent. We have found that Mg2+ is important in the coat assembly reaction. At pH 8 in 0.01 M or 0.1 M Tris, coats dissociate; however, 10 mM MgCl2 prevents dissociation. If the coats are first dissociated at pH 8 and then the MgCl2 raised to 10 mM, reassembly occurs. These results suggest that Mg2+ stabilizes the coat lattice and promotes reassembly. This hypothesis is supported by our observations that increasing Mg2+ (10 μM-10 mM) increases reassembly whereas chelation of Mg2+ by (EGTA) inhibits reassembly. Coats reassembled in low-Tris (0.01 M, pH 8) supernatants containing 10 mM MgCl2 do not sediment, but upon dialysis into isolation buffer (pH 6.8), these coats become sedimentable. Nonsedimentable coats are noted also either when partially purified clathrin (peak I from Sepharose CL4B columns) is dialyzed into low-ionic-strength buffer or when peaks I and II are dialyzed into isolation buffer. Such nonsedimentable coats may represent intermediates in the assembly reaction which have normal morphology but lack some of the physical properties of native coats. We present a model suggesting that tightly intertwined antiparallel clathrin dimers form the edges of the coat lattice.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jss.400110213
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 8
    Electronic Resource
    Electronic Resource
    Selective protein transport: Identity of the solubilized phosvitin receptor from chicken oocytes (1980)
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 14 (1980), S. 473-481 
    Details
    ISSN: 0091-7419
    Keywords: protein transport ; phosvitin ; receptor ; coated vesicles ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: By two independent methods, the solubilized receptor for phosvitin (PV) has a subunit MW of 116K. Affinity chromatography, showed that only 2 of the more than 25 proteins present in the total detergent solubilized oocyte membrane extract were retained on a PV-agarose column. These proteins of MW of 116K and 100K could be eluted from PV-agarose with free PV. By gel exclusion chromatography, the receptor-125I-PV complexes elute in the void volume of a Biogel A-1.5 column. When these void fractions were assayed by SDS-PAGE only a single protein of MW of 116K was observed in addition to 125I-PV.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jss.400140406
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 9
    Electronic Resource
    Electronic Resource
    Binding to specific receptors on oocyte plasma membranes by serum phosvitin-lipovitellin (1976)
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 4 (1976), S. 89-97 
    Details
    ISSN: 0091-7419
    Keywords: Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Specific binding sites for the serum complex of phosvitin and lipovitellin have been shown to exist on the outer surface of rapidly growing chicken oocytes. The existence and specificity of these sites were demonstrated by competition for binding to unfixed oocyte membrane fragments and by displacement of already bound and labeled phosvitin-lipovitellin from formaldehyde-fixed membranes. Only unlabeled phosvitin-lipovitellin competed with the 125I-labeled complex for binding to the fragments or displacement of bound label; IgG isolated from egg yolks and bovine serum albumin were ineffective.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jss.400040109
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 10
    Electronic Resource
    Electronic Resource
    Selective protein transport: Characterization and solubilization of the phosvitin receptor from chicken oocytes (1979)
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 12 (1979), S. 491-504 
    Details
    ISSN: 0091-7419
    Keywords: oocyte protein transport ; receptor solubilization ; phosvitin receptor ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Phosvitin (PV), a subunit of a female-specific protein, vitellogenin, binds to oocyte membranes with a KD of 10-6 M. Binding reaches equilibrium within 30 min after incubation at 25°C. Bound 125I-PV dissociates from the membrane with a t1/2 of 13 h when incubated in buffer. However, when 125I-PV-labeled membranes are incubated in buffer containing 10-5 M unlabeled PV, 50% of the initially bound 125I-PV dissociates from the membrane within 10 min. These results support the conclusion that PV binds to a membrane-associated receptor.Solubilization studies show that Triton X-100 solubilizes up to 45% of the total membrane-bound 125I-PV. Gel-exculsion chromatography of the solubilized material yields a 500,000 dalton 125I-PV-containing complex separated from free 125I-PV. The 500,000 dalton complex completely dissociates to yield free 125I-PV when incubated with excess unlabeled PV. However, when incubated with (1) no addition, (2) IgG, or (3) serum albumin, the extent of dissociation is significantly reduced and is consistent with that which would be predicted on the basis of the observed dissociation rate in the absence of unlabeled PV.These results suggest that bound 125I-PV can only be displaced by unlabeled PV. These results also indicate that the 500,000 dalton species is a solubilized PV-receptor complex and that it is possible to solubilize the PV-receptor in an active form.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jss.400120409
    Location Call Number Limitation 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...