Primary Structure of Protein L10 from the Large Subunit ofEscherichia coliRibosomes

التفاصيل البيبلوغرافية
العنوان: Primary Structure of Protein L10 from the Large Subunit ofEscherichia coliRibosomes
المؤلفون: Dieter Brauer, Ingeborg Heiland, Brigitte Wittmann-Liebold
المصدر: Hoppe-Seyler´s Zeitschrift für physiologische Chemie. 357:1751-1770
بيانات النشر: Walter de Gruyter GmbH, 1976.
سنة النشر: 1976
مصطلحات موضوعية: Ribosomal Proteins, Chemical Phenomena, medicine.medical_treatment, Phthalic Acids, Thermolysin, Carboxypeptidases, Biochemistry, chemistry.chemical_compound, Bacterial Proteins, Escherichia coli, medicine, Chymotrypsin, Trypsin, Amino Acid Sequence, Cyanogen Bromide, Amino Acids, Peptide sequence, Protease, Edman degradation, biology, Protein primary structure, Chemistry, chemistry, biology.protein, Cyanogen bromide, Peptides, Eukaryotic Ribosome, Peptide Hydrolases, medicine.drug
الوصف: The complete primary structure of protein L10 from the large subunit of the Escherichia coli ribosome has been determined. L10 is composed of 165 residues and has the amino acid composition: Asp6, Asn3, Thr9, Ser6, Glu14, Gln4, Pro5, Gly9, Ala33, Val15, Met5, Ile5, Leu15, Tyr3, Phe6, His1, Lys12, Arg13 and Cys1. The molecular weight of L10 is 17 738. The amino acid sequence was determined by a combination of automated Edman degradation of the intact protein in a modified Beckman sequentor and sequencing peptides obtained from digestions with trypsin, themolysin, Staphylococcus aureus protease and chymotrypsin. Further information was obtained from cyanogen bromide fragments and peptides resulting from digestion with trypsin after protection of the epsilon-amino groups of the lysine residues with exo-cis-3,6-endoxo-delta4-tetrahydrophthalic anhydride (ETPA).
تدمد: 0018-4888
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a8b177f4ff3cdbfd7894f425df7cc907Test
https://doi.org/10.1515/bchm2.1976.357.2.1751Test
رقم الانضمام: edsair.doi.dedup.....a8b177f4ff3cdbfd7894f425df7cc907
قاعدة البيانات: OpenAIRE