scholarly journals Studies on the primary structure of .ALPHA.-amylase from Bacillus subtilis var. amylosacchariticus. Part II. Isolation and amino acid sequences of tryptic peptides of .ALPHA.-amylase from Bacillus subtilis var. amylosacchariticus.

1985 ◽  
Vol 49 (7) ◽  
pp. 1911-1922 ◽  
Author(s):  
Yoshiho NAGATA ◽  
Shigeto SUGA ◽  
Bunji MARUO
Keyword(s):  
Bacillus Subtilis ◽  
Amino Acid ◽  
Primary Structure ◽  
Amino Acid Sequences ◽  
Alpha Amylase ◽  
Tryptic Peptides

scholarly journals Sequence of the N-terminal half of Bacillus amyloliquefaciens α-amylase

1980 ◽  
Vol 185 (2) ◽  
pp. 387-395 ◽  
Author(s):  
H Chung ◽  
F Friedberg
Keyword(s):  
Amino Acids ◽  
Bacillus Subtilis ◽  
Amino Acid ◽  
Aspartic Acid ◽  
Primary Structure ◽  
Bacillus Amyloliquefaciens ◽  
Proteolytic Enzymes ◽  
Alpha Amylase ◽  
Sequence Determination ◽  
N Terminus

Bacillus amyloliquefaciens alpha-amylase (1,4-alpha-D-glucan glucanohydrolase. EC 3.2.1.1), which is commercially supplied as ‘Bacillus subtilis alpha-amylase’ does not cross-react immunologically with B. subtilis alpha-amylase. This enzyme (from B. amyloliquefaciens) was cleaved by treatment with CNBr into seven fragments. Peptide A was selected for sequence determination. It is the longest one, containing 185 amino acids (i.e. approx. 50% of the total molecule) and connects to the hexapeptide of the N-terminus. Its primary structure was aligned by use of various proteolytic enzymes. The sequence of amino acids 181-184 is identical with that of amino acids 14-17 of the alpha-amylase isolated from B. subtilis (except that amino acid 183 is asparagine rather than aspartic acid).

Die primäre Proteinstruktur von Stämmen des Tabakmosaikvirus

1969 ◽  
Vol 24 (7) ◽  
pp. 870-877 ◽  
Author(s):  
J. Jauregui-Adell ◽  
I. Hindennach ◽  
H. G. Wittmann
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Coat Protein ◽  
Tobacco Mosaic Virus ◽  
Primary Structure ◽  
Amino Acid Sequences ◽  
The Other ◽  
Protein Subunit ◽  
Tryptic Peptides ◽  
Tmv Strains

The sequence of amino acids within the coat protein of the strain Holmes rib grass of tobacco mosaic virus (TMV) has been determined. In this communication the amino acid compositions of the coat protein and of all tryptic peptides are reported. Furthermore the experimental details are given for the elucidation of the amino acid sequences within the first three tryptic peptides, containing 61 amino acids.It has been found that the strain Holmes rib grass differs very extensively in the primary structure from the other TMV strains whose sequences are known. It differs from each of the other strains in more than 50% of the amino acid positions and it contains two amino acids less per protein subunit than the other TMV strains.

Embryonale Hämoglobine der Säuger: Die Sequenzen der ζ-, ε-und ϑ-Ketten vom Hausschwein (Sus scrofa domestica) Embryonic Hemoglobins in Mammals: The Primary Structures of e-and 5-Chains of the Pig (Sus scrofa dom estica) / Embryonic Hemoglobins in Mammals: The Primary Structures of ζ-, ε-and ϑ-Chains of the Pig (Sms scrofa domesrica)

1983 ◽  
Vol 38 (7-8) ◽  
pp. 613-616 ◽  
Author(s):  
F. A. Bieber ◽  
H. Aschauer ◽  
S. M. Bektas ◽  
G. Braunitzer
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Primary Structure ◽  
Sus Scrofa ◽  
Globin Gene ◽  
Amino Acid Sequences ◽  
Tryptic Peptides ◽  
Primary Structures ◽  
Sus Scrofa Domestica

The amino-acid sequences of all expressed hemoglobins of the pig embryo are given: Hemo­globin Gower I (ζ2/ε2), Hemoblobin Gower II (α2/ε2), Hemoglobin Heide I (ζ2/ϑ2) and Hemo­globin Heide II (α0/ϑ2). The ζ-, ε- and ϑ-chains were obtained with chromatography on CM-cellulose from isolated hemoglobin components. The primary structure was established by sequencing the tryptic peptides in the sequenator: they where isolated using HPLC. The ζ-chains from pig and human differ in 23, the ε-chains in 20 positions. The embryonic globin-gene which express the ϑ-chains, is a new one in mammals, of ε-type and up to now it could only be found in pigs: the amino-acid sequence differ in only 4 positions from the ε-chains. Because no γ-chains (fetal Hb) are expressed the sequences of all hemoglobins (5 hemoglobin chains forming 5 different hemo­globins) of ontogeny in pig are now described.

scholarly journals Differences in the Amino Acid Sequences of Tryptic Peptides from Three Sheep Hemoglobin β Chains

1967 ◽  
Vol 242 (9) ◽  
pp. 2211-2232
Author(s):  
Samuel H. Boyer ◽  
Peter Hathaway ◽  
Flora Pascasio ◽  
James Bordley ◽  
Charlene Orton ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequences ◽  
Tryptic Peptides ◽  
Sheep Hemoglobin

scholarly journals The primary structure of aspartate aminotransferase from pig heart muscle. Partial sequences determined by digestion with thermolysin and elastase

1973 ◽  
Vol 133 (4) ◽  
pp. 805-819 ◽  
Author(s):  
Francesco Bossa ◽  
Donatella Barra ◽  
Massimo Carloni ◽  
Paolo Fasella ◽  
Francesca Riva ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Primary Structure ◽  
Aspartate Aminotransferase ◽  
Heart Muscle ◽  
Science And Technology ◽  
Amino Acid Sequences ◽  
Amino Acid Residues ◽  
Lending Library

Peptides produced by thermolytic digestion of aminoethylated aspartate aminotransferase and of the oxidized enzyme were isolated and their amino acid sequences determined. Digestion by elastase of the carboxymethylated enzyme gave peptides representing approximately 40% of the primary structure. Fragments from these digests overlapped with previously reported sequences of peptides obtained by peptic and tryptic digestion (Doonan et al., 1972), giving ten composite peptides containing 395 amino acid residues. The amino acid composition of these composite peptides agrees well with that of the intact enzyme. Confirmatory results for some of the present data have been deposited as Supplementary Publication 50018 at the National Lending Library for Science and Technology, Boston Spa, Yorks. LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1973) 131, 5.

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