Primary structures of three highly acidic ribosomal proteins S6, S12 and S15 from the archaebacterium Halobacterium marismortui
作者： Junko Kimura , Evelyn Arndt , Makoto Kimura
DOI: 10.1016/0014-5793(87)80423-4
关键词: Biology 、 Sequence analysis 、 Peptide sequence 、 Biochemistry 、 Protease 、 Protein primary structure 、 Ribosomal protein 、 Halobacterium 、 Chymotrypsin 、 Amino acid 、 Molecular biology
摘要: The amino acid sequences of three extremely acidic ribosomal proteins, S6, S12, and S15, from Halobacterium marismortui have been determined. were obtained by the sequence analysis peptides derived enzymatic digestion with trypsin. Stapylococcus aureus protease chymotrypsin, as well cleavage dilute HCl. S12 consist 116, 147 102 residues, molecular masses 12251, 16440 11747 Da, respectively. Comparison these proteins protein other organisms revealed that halobacterial has homology eukaryotic S16A Saccharomyces cerevisiae, while S15 is significantly related to Xenopus laevis S19 protein. No was found between any eubacterial proteins.
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