Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Abdolreza Kamyab"'
Publikováno v:
The Journal of Poultry Science, Vol 44, Iss 3, Pp 322-329 (2007)
The interaction between chick type and xylanase supplementation (Avizyme 1300) of a wheat based diet was investigated using a 3×2 factorial arrangement. The diet (645g wheat/kg) was supplemented with 0 or 1g/kg xylanase and fed to broilers, broiler
Externí odkaz:
https://doaj.org/article/7e9745c2b2bc458fa431991843af5b33
Publikováno v:
Korean Journal of Poultry Science. 38:191-195
The objectives of this study are to identify specific functional genes which are related with growth and protein structure of the pectoral muscle of Korean native chicken. Pectoral muscle was isolated from three Korean native chickens (KNC, red brown
Publikováno v:
The Journal of Poultry Science. 44:322-329
The interaction between chick type and xylanase supplementation (Avizyme 1300) of a wheat based diet was investigated using a 3×2 factorial arrangement. The diet (645g wheat/kg) was supplemented with 0 or 1g/kg xylanase and fed to broilers, broiler
Autor:
Abdolreza Kamyab
Publikováno v:
World's Poultry Science Journal. 57:5-12
The constant economic pressure on poultry producers to lower their costs and increase the quality of their products has been a big challenge in today's competitive world. Moreover, the confirment of turkeys has been linked with several kinds of breas
Publikováno v:
Plant Physiology. 99:538-547
Earlier we isolated a threonine-rich extensin from maize (Zea mays). Here, we report that maize cell suspension cultures yield a new extensin rich in histidine (HHRGP) that also has characteristics of arabinogalactan proteins (AGPs). Thus, chymotrypt
Autor:
Abdolreza Kamyab, Michael A. Held, Elena D. Shpak, Li Tan, Marcia J. Kieliszewski, Michael Hare
Publikováno v:
The Journal of biological chemistry. 279(53)
Extensins are cell wall hydroxyproline-rich glycoproteins that form covalent networks putatively involving tyrosyl and lysyl residues in cross-links catalyzed by one or more extensin peroxidases. The precise cross-links remain to be chemically identi