scholarly journals Amino acid sequence of flagellin of Bacillus subtilis 168. III. Tryptic peptides, N-bromosuccinimide peptides, and the complete amino acid sequence.

1976 ◽  
Vol 251 (3) ◽  
pp. 705-711
Author(s):  
R J DeLange ◽  
J Y Chang ◽  
J H Shaper ◽  
A N Glazer
Keyword(s):  
Bacillus Subtilis ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Tryptic Peptides ◽  
Complete Amino Acid Sequence ◽  
Bacillus Subtilis 168

scholarly journals On the Amino-Acid Sequence of Flagellin from Bacillus subtilis 168: Comparison with Other Bacterial Flagellins

1973 ◽  
Vol 70 (12) ◽  
pp. 3428-3431 ◽  
Author(s):  
R. J. Delange ◽  
J. Y. Chang ◽  
J. H. Shaper ◽  
R. J. Martinez ◽  
S. K. Komatsu ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Bacillus Subtilis 168

scholarly journals Identical amino acid sequence of the aroA(G) gene products of Bacillus subtilis 168 and B. subtilis Marburg strain

Microbiology ◽  
1995 ◽  
Vol 141 (9) ◽  
pp. 2219-2222 ◽  
Author(s):  
A. Bolotin ◽  
V. Khazak ◽  
N. Stoynova ◽  
K. Ratmanova ◽  
Y. Yomantas ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Gene Products ◽  
Bacillus Subtilis 168 ◽  
Identical Amino Acid ◽  
Identical Amino Acid Sequence

scholarly journals The complete amino acid sequence of a mouse ϰ light chain

1972 ◽  
Vol 128 (2) ◽  
pp. 427-444 ◽  
Author(s):  
J. Svasti ◽  
C. Milstein
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
Paper Electrophoresis ◽  
Tryptic Peptides ◽  
Myeloma Protein ◽  
Complete Amino Acid Sequence ◽  
Cellulose Column ◽  
Mouse Myeloma

The complete amino acid sequence of the κ-chain of the mouse myeloma protein MOPC 21 was established. The protein was reduced and alkylated with iodo[2-14C]acetic acid, and 21 tryptic peptides were isolated, mainly by paper electrophoresis and paper chromatography. Three large tryptic peptides (of 35, 36 and 42 residues), which were difficult to isolate in this manner, were obtained pure and in excellent yields by a combination of Sephadex G-50 gel filtration in 1% (w/v) NH4HCO3 and chromatography on a DEAE-cellulose column in ammonium acetate buffer, pH8.1. Peptides overlapping the tryptic peptides were isolated from a chymotryptic digest. The chain is 214 residues long. Microheterogeneity of two peptides was observed and is believed to be due to deamidation. It was not excluded that such deamidation could occur in serum from which the protein was isolated. The sequence is compared with the sequences of two other mouse κ-chains, and with the human κ-chain basic sequences.

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