Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Ray-Jen Chang"'
Autor:
Eirik Nestaas, Vafa Lahidji, William S. Hancock, Peter K. Murakami, Michael Mccaman, Elisabeth Lehmberg, Ray-Jen Chang, Erno Pungor, Maria Parkman, John A Chakel, Joseph A. Traina, Jeffrey W. Nelson
Publikováno v:
Journal of Chromatography B: Biomedical Sciences and Applications. 732:411-423
An RP-HPLC assay was developed for a recombinant adenovirus type 5. During chromatography, intact adenovirus dissociated into its structural components (DNA and proteins) and the viral proteome was separated yielding a characteristic fingerprint. The
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3f0432e88e2e125383d46e6028149b64
https://doi.org/10.1016/s0378-4347(99)00316-3
https://doi.org/10.1016/s0378-4347(99)00316-3
Publikováno v:
Journal of Bacteriology. 180:444-448
A tandem pair of nearly identical genes from Serpulina hyodysenteriae (B204) were cloned and sequenced. The full open reading frame of one gene and the partial open reading frame of the neighboring gene appear to encode secreted proteins which are ho
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::794e83dd971d67d9386c828519e300c8
https://doi.org/10.1128/jb.180.2.444-448.1998
https://doi.org/10.1128/jb.180.2.444-448.1998
Publikováno v:
Journal of Biological Chemistry. 267:2325-2328
A unique form of transforming growth factor-beta (TGF-beta), TGF-beta 2.3 heterodimer, has been purified from bovine bone extract. TGF-beta 2.3 migrated as a single 25-kDa band by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, whereas und
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::59066005b9352edda455afadc77a9abe
https://doi.org/10.1016/s0021-9258(18)45881-4
https://doi.org/10.1016/s0021-9258(18)45881-4
Publikováno v:
Infection and immunity. 63(1)
Extracytoplasmic proteins were released from Serpulina (Treponema) hyodysenteriae (strain B204) by treatment of whole cells with a nonionic detergent (Tween 20). Centrifugation of the Tween 20-released proteins at 100,000 x g sedimented 10 major extr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::73a28a90a9fe476fc9201f7629faa7f9
https://pubmed.ncbi.nlm.nih.gov/7806350
https://pubmed.ncbi.nlm.nih.gov/7806350