نتایج جستجو برای: ribosomal proteins

تعداد نتایج: 582395  

Journal: :European Journal of Biochemistry 1978

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1974
C C Liew C C Yip

When rabbit reticulocytes were incubated in vitro with [(3)H]acetate, their ribosomal proteins were rapidly acetylated within 10 min. Polyacrylamide-urea gel electrophoresis showed that several major ribosomal protein fractions were highly acetylated. By the double-isotope labeling technique, the incorporation of [(3)H]acetate and [(14)C]aminoacid mixture into ribosomal proteins and nascent cha...

Journal: :Molecular biology and evolution 1984
R J Schmidt A M Myers N W Gillham J E Boynton

Polyclonal antibodies were elicited against seven of the 33 different proteins of the large subunit of the chloroplast ribosome from Chlamydomonas reinhardtii. Three of these proteins are synthesized in the chloroplast and four are made in the cytoplasm and imported. In western blots, six of the seven antisera are monospecific for their respective large subunit ribosomal proteins, and none of t...

2015
Patrick Pausch Ujjwala Singh Yasar Luqman Ahmed Benjamin Pillet Guillaume Murat Florian Altegoer Gunter Stier Matthias Thoms Ed Hurt Irmgard Sinning Gert Bange Dieter Kressler

Exponentially growing yeast cells produce every minute >160,000 ribosomal proteins. Owing to their difficult physicochemical properties, the synthesis of assembly-competent ribosomal proteins represents a major challenge. Recent evidence highlights that dedicated chaperone proteins recognize the N-terminal regions of ribosomal proteins and promote their soluble expression and delivery to the as...

2002
F. PHILLIPS EDWIN H. MCCONKEY

Total protein was released from isolated HeLa cell nucleoli by guanidine hydrochloride, purified by cesium chloride density gradient centrifugation, and analyzed by two-dimensional polyacrylamide gel electrophoresis. Conditions of electrophoresis restricted attention to proteins that are positively charged at pH 8.6. Most of the major nucleolar protein spots co-electrophoresed with ribosomal pr...

Journal: :The Journal of biological chemistry 1976
W F Phillips E H McConkey

Total protein was released from isolated HeLa cell nucleoli by guanidine hydrochloride, purified by cesium chloride density gradient centrifugation, and analyzed by two-dimensional polyacrylamide gel electrophoresis. Conditions of electrophoresis restricted attention to proteins that are positively charged at pH 8.6. Most of the major nucleolar protein spots co-electrophoresed with ribosomal pr...

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