NDLI: Determination of the Complete Amino-Acid Sequence of Protein S4 from Escherichia coli Ribosomes

Content Provider	Scilit
Author	Schiltz, Emil Reinbolt, Joseph
Copyright Year	1975
Description	Journal: Journal of Biological Inorganic Chemistry After digestion of protein S4 with trypsin, all 32 tryptic peptides were isolated. Their amino acid compositions were analyzed and the sequence of the amino acids within the tryptic peptides was determined by means of a solid-phase peptide sequenator and by exopeptidases. Alignment of the tryptic peptides was established by analyzing and partially sequencing peptides isolated after digestion of the S4 protein with chymotrypsin, thermolysin and a glutamic-acid-specific protease. Further information about the alignment of peptides came from treatment of S4 with CNBr and with a lysine-modifying reagent.
Ending Page	481
Starting Page	467
ISSN	2573508X
e-ISSN	14321327
DOI	10.1111/j.1432-1033.1975.tb02253.x
Journal	Journal of Biological Inorganic Chemistry
Issue Number	2
Volume Number	56
Language	English
Publisher	Wiley-Blackwell
Publisher Date	1975-08-01
Access Restriction	Open
Subject Keyword	Journal: Journal of Biological Inorganic Chemistry Biochemical Research Amino Acid
Content Type	Text
Resource Type	Article
Subject	Biochemistry Inorganic Chemistry

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Determination of the Complete Amino-Acid Sequence of Protein S4 from Escherichia coli Ribosomes