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
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 52 (1989), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Ependymins are thought to be implicated in fundamental processes involved in plasticity of the goldfish CNS. Gas-phase sequencing of purified ependymins β and γ revealed that they share the same N-terminal sequence. Each sequence displays microheterogeneities at several positions. Based on the protein sequences obtained, we constructed synthetic oligonucleotides and used them as hybridization probes for screening cDNA libraries of goldfish brain. In this article we describe the full-length sequence of a mRNA encoding a precursor of ependymins. A cleavable signal sequence characteristic of secretory proteins is located at the N-terminal end, followed directly by the ependymin sequence. Also, two potential N-glycosylation sites were detected. A computer search revealed that ependymins form a novel family of unique proteins.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 2
    Electronic Resource
    Electronic Resource
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Environment and Resources 1 (1976), S. 37-63 
    ISSN: 0362-1626
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Energy, Environment Protection, Nuclear Power Engineering
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 3
    Electronic Resource
    Electronic Resource
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 89 (1988), S. 197-203 
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Notes: The corrections to the equilibrium rate of the chemical reaction A+B→products are analyzed for the Lorentz gas composed of light particles A reacting with heavy particles B in the presence of heavy particles of a carrier gas C. Particles B and C are treated as a heat bath. The reaction is analyzed under conditions in which the products can be neglected. The model of reacting hard spheres (line-of-centers model) introduced by Present is used. Analysis is performed in two ways: (1) By obtaining analytical expressions following from the Chapman–Enskog perturbation solution of the Boltzmann equation generalized for gases reacting chemically. (2) By obtaining numerical results which follow from a numerical solution of a partial differential equation which can be derived from the Boltzmann equation for the reactive Lorentz gas. It is shown that for a specified region of system parameters both types of solution of the Boltzmann equation coincide. The comparison of both methods permits us to find out under which conditions the perturbation method of solution may be used.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 4
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    The @journal of physical chemistry 〈Washington, DC〉 93 (1989), S. 466-468 
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 5
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    The @journal of physical chemistry 〈Washington, DC〉 93 (1989), S. 4507-4511 
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 6
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of the American Chemical Society 109 (1987), S. 6976-6981 
    ISSN: 1520-5126
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 7
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food processing and preservation 1 (1977), S. 0 
    ISSN: 1745-4549
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Protein blends were prepared from peanut flour or peanut protein concentrate and whey protein concentrate, sodium caseinate, calcium caseinate or nonfat dry milk. One per cent protein dispersions of these blends containing 0.0, 25.0, 50.0, and 100.0% peanut protein were heated at 60, 80, and 90° C for 30 min. Soluble protein was lower in unheated peanut protein preparations than in unheated milk proteins preparations with lowest soluble protein observed in peanut flour dispersions. Solubility of milk proteins dispersed in distilled water was generally not affected by heat treatment, while heating of similarly prepared peanut protein dispersions above 80° C decreased soluble protein. Systems containing peanut protein with whey protein calcium caseinate or nonfat dry milk were intermediate, in soluble protein and heat stability to that of milk and peanut proteins alone. Soluble protein in peanut/sodium caseinate blends increased slightly with heat treatment. Calcium addition to 30mM decreased soluble protein in all protein systems. Peanut lipoprotein concentrate was not affected by added calcium. Heating whey protein, caseinate and blends of peanut with whey or caseinate in the presence of calcium induced aggregation and lowered soluble protein.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 8
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Journal of the American Chemical Society 98 (1976), S. 8181-8185 
    ISSN: 1520-5126
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 9
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food processing and preservation 2 (1978), S. 0 
    ISSN: 1745-4549
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Time required for gelation of 10% protein dispersions of commercial whey protein concentrate (WPC) heated at 100°C was influenced by preparation technique. Gel times ranged from 1.25 to greater than 30 min. Dialysis of a rapid gelling WPC resulted in the formation of stronger, more cohesive, less springy, more gummy, more chewy and more translucent gels with heating (100° C for 15 min) at 10% protein than did non-dialyzed WPC. Addition of CaCl2 or NaCl to the dialyzed WPC increased gel strength more dramatically than did salt addition to non-dialyzed WPC. Resistance to penetration and hardness of dialyzed whey protein gels maximized with CaCl2 addition from 5.0 to 20 mM and decreased with 25 mM CaCl2 addition. In non-dialyzed whey protein gels, resistance to penetration maximized at 25 mM added CaCl2 while hardness values maximized at 5.0 mM CaCl2. Addition of 0.2 to 0.5 M NaCl increased resistance to penetration of both whey protein gel systems. Hardness values for dialyzed WPC gels maximized at 0.1 to 0.3 M NaCl and decreased at 0.4 M or greater added NaCl. Hardness values of non-dialyzed WPC were only slightly affected by NaCl addition. Addition of CaCl2 at 5 mM or greater or NaCl at 0.1 Af or greater decreased cohesiveness and springiness of dialyzed WPC gels. Cohesiveness of non-dialyzed WPC gel systems was maximal at 10 mM CaCl2 or 0.2M NaCl. Salt had no apparent effect on springiness of the non-dialyzed WPC gels. Gumminess data followed similar trends to those observed for hardness with respect to salt effects in WPCgel systems. Maximum chewiness values for both WPC gel systems were apparent with addition of 5.0 to 10 mM CaC12 or with addition of0.1 to 0.3 M NaCl.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
  • 10
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 43 (1978), S. 0 
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Whey protein concentrate dispersions formulated at 7.5% or more of protein formed strong gels when heated at temperatures above 80°C. Quantitative gel strength calculated from penetration force data generally increased with heating temperature to 110°C. Increasing pH from 7.0 to 9.0 generally decreased the gel strength of whey protein concentrate. At a total protein concentration of 10%, gel strength was lower when peanut flour protein was 25% or more of a mixture with whey protein. Only weak gels were formed with heating protein blends formulated with peanut protein at greater than 50% of total protein. Sodium chloride (up to 0.5M) and calcium chloride (up to 30 mM) increased gel strength of whey protein and blended systems, but decreased gel strength of dispersions containing only peanut flour. Calcium chloride at 30 mM destroyed gelation ability of peanut flour causing protein precipitation. Gel strength of whey protein increased with moderate cysteine addition and was maximum at a level of 25 mM cysteine. Addition of 100 mM cysteine dramatically reduced whey protein gel strength. Cysteine addition decreased gel strength of peanut flour dispersions and had a varied effect on blended protein systems.
    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...