ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

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
    Genetic Diversity of Cattle in South China as Revealed by Blood Protein Electrophoresis (1999)
    Springer
    Biochemical genetics 37 (1999), S. 257-265 
    Details
    ISSN: 1573-4927
    Keywords: CATTLE ; MITHAN ; BOS FRONTALIS ; SOUTH CHINA ; BLOOD PROTEIN ELECTROPHORESIS ; GENETIC ; DIVERSITY
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Genetic variation of 31 blood protein loci in236 cattle from eight South China populations (includingmithan, Bos frontalis) and a Holstein population wasinvestigated by means of horizontal starch gel electrophoresis. Thirteen loci (ALB, CAR, Hb-b,Np, PGM, Amy-I, PEP-B, AKP, 6PGD, Cp, Pa, EsD, and TF)were found to be polymorphic. The comparison of averageheterozygosities (H) shows that all the native cattle embrace a rich genetic diversity. Ourresults on protein polymorphism suggest that cattle inChina originated mainly from Bos indicus and Bos taurus;Xuwen, Hainan, Wenshan, and Dehong cattle and the Dehong zebu are close to zebu-type cattle,and Diqing and Zhaotong cattle are close to the taurine.The mithan was very different from other native cattle,and we suggest that its origin was complicated and may be influenced by other cattlespecies.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1018798924778
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Solid-phase synthesis of triple-helical collagen-model peptides (1996)
    Springer
    International journal of peptide research and therapeutics 3 (1996), S. 3-16 
    Details
    ISSN: 1573-3904
    Keywords: Cell adhesion ; Collagen ; Peptide amphiphiles ; Triple-helical peptides
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary The triple-helical conformation of collagen has been proposed to be important for mediation of cellular activities, such as adhesion and activation, extracellular matrix assembly, and enzyme function. We have developed synthetic protocols that allow for the study of biological activities of specific collagen sequences in triple-helical conformation. These methods primarily involve solid-phase assembly and covalent linkage of three peptide chains. The resultant triple-helical peptides have sufficient thermal stabilities to permit structural and biological characterization under physiological conditions. The present article critically reviews the various approaches for constructing synthetic triple-helices.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00131080
    Location Call Number Expected 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...