Type your tag names separated by a space and hit enter

Purification and properties of Haemophilus paragallinarum hemagglutinin.

Abstract

Hemagglutinin (HA) of Haemophilus paragallinarum was purified, and its immunologic, chemical, and morphologic properties were studied. The HA was purified by gel filtration on Sepharose 6B and by subsequent ultracentrifugation of trypsinized cells after pretreatment with neuraminidase. After gel filtration, the HA component (fractioned HA) gave 1 precipitin line by gel diffusion, and after inoculation in chickens, hemagglutinination-inhibition antibody to trypsin-sensitive HA antigen was found. Chickens inoculated with the fractionated HA were protected from challenge exposure with H paragallinarum. In a sample further purified by ultracentrifugation (purified HA), a single protein band was detected by sodium dodecyl sulfate-polyacrylamide gel electrophoresis; it had a molecular weight of approximately 39,000. A molecular weight of several hundred thousand to several million was observed by gel filtration. Seemingly, HA of H paragallinarum is an aggregate of more than 20 HA sub-units. The purified HA included protein and some sugars, and according to electron microscopic observation, had a filamentous structure.

Links

  • patent databases
  • Authors

    , ,

    Source

    MeSH

    Animals
    Chickens
    Electrophoresis, Polyacrylamide Gel
    Haemophilus
    Hemagglutination Tests
    Hemagglutinins
    Microscopy, Electron
    Molecular Weight

    Pub Type(s)

    Comparative Study
    Journal Article

    Language

    eng

    PubMed ID

    7212446

    Citation

    Iritani, Y, et al. "Purification and Properties of Haemophilus Paragallinarum Hemagglutinin." American Journal of Veterinary Research, vol. 41, no. 12, 1980, pp. 2114-8.
    Iritani Y, Katagiri K, Arita H. Purification and properties of Haemophilus paragallinarum hemagglutinin. Am J Vet Res. 1980;41(12):2114-8.
    Iritani, Y., Katagiri, K., & Arita, H. (1980). Purification and properties of Haemophilus paragallinarum hemagglutinin. American Journal of Veterinary Research, 41(12), pp. 2114-8.
    Iritani Y, Katagiri K, Arita H. Purification and Properties of Haemophilus Paragallinarum Hemagglutinin. Am J Vet Res. 1980;41(12):2114-8. PubMed PMID: 7212446.
    * Article titles in AMA citation format should be in sentence-case
    TY - JOUR T1 - Purification and properties of Haemophilus paragallinarum hemagglutinin. AU - Iritani,Y, AU - Katagiri,K, AU - Arita,H, PY - 1980/12/1/pubmed PY - 1980/12/1/medline PY - 1980/12/1/entrez SP - 2114 EP - 8 JF - American journal of veterinary research JO - Am. J. Vet. Res. VL - 41 IS - 12 N2 - Hemagglutinin (HA) of Haemophilus paragallinarum was purified, and its immunologic, chemical, and morphologic properties were studied. The HA was purified by gel filtration on Sepharose 6B and by subsequent ultracentrifugation of trypsinized cells after pretreatment with neuraminidase. After gel filtration, the HA component (fractioned HA) gave 1 precipitin line by gel diffusion, and after inoculation in chickens, hemagglutinination-inhibition antibody to trypsin-sensitive HA antigen was found. Chickens inoculated with the fractionated HA were protected from challenge exposure with H paragallinarum. In a sample further purified by ultracentrifugation (purified HA), a single protein band was detected by sodium dodecyl sulfate-polyacrylamide gel electrophoresis; it had a molecular weight of approximately 39,000. A molecular weight of several hundred thousand to several million was observed by gel filtration. Seemingly, HA of H paragallinarum is an aggregate of more than 20 HA sub-units. The purified HA included protein and some sugars, and according to electron microscopic observation, had a filamentous structure. SN - 0002-9645 UR - https://www.unboundmedicine.com/medline/citation/7212446/Purification_and_properties_of_Haemophilus_paragallinarum_hemagglutinin_ L2 - https://www.lens.org/lens/search?q=citation_id:7212446 DB - PRIME DP - Unbound Medicine ER -