scholarly journals The primary structure of aspartate aminotransferase from pig heart muscle. Digestion with a proteinase having specificity for lysine residues

1975 ◽  
Vol 149 (3) ◽  
pp. 497-506 ◽  
Author(s):  
S Doonan ◽  
H J Doonan ◽  
R Hanford ◽  
C A Vernon ◽  
J M Walker ◽  
...  
Keyword(s):  
Primary Structure ◽  
Aspartate Aminotransferase ◽  
The Other ◽  
British Library ◽  
Side Chains ◽  
Amino Acid Residues ◽  
Main Paper ◽  
Lysine Residues ◽  
Arginine Residues ◽  
Complete Primary Structure

Carboxymethylated aspartate aminotransferase was digested with a proteinase claimed to be specific for lysine residues. Complete cleavage occurred at 12 of the 19 lysine residues in the protein, but at the remaining seven residues cleavage was either restricted or absent. In addition, cleavage was observed at three of the 26 arginine residues. These results are discussed with reference to the amino acid residues adjacent to points of complete or restricted cleavage. The complete primary structure of aspartate aminotransferase, based on these and other studies, is given. Evidence for the assignment of some acid and amide side chains has been deposited as Supplementary Publication SUP 50050 (11 pp.) at the British Library (Lending Division), Boston Spa, Wetherby, W. Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1975) 145, 5. The evidence for the assignment of residue 366 was less conclusive than for the other acid and amide side chains and is, therefore, given in the main paper.

scholarly journals The primary structure of histone H2A from the nematode Caenorhabditis elegans

1987 ◽  
Vol 243 (1) ◽  
pp. 297-300 ◽  
Author(s):  
J R Vanfleteren ◽  
S M Van Bun ◽  
J J Van Beeumen
Keyword(s):  
Amino Acid ◽  
Caenorhabditis Elegans ◽  
Primary Structure ◽  
Amino Acid Residues ◽  
Histone H2a ◽  
Nematode Caenorhabditis Elegans ◽  
Calf Thymus ◽  
N Terminus ◽  
Lysine Residues ◽  
Complete Primary Structure

The complete primary structure of histone H2A from the nematode Caenorhabditis elegans was determined. The amino acid chain consists of 126 amino acid residues and has a blocked N-terminus. By comparison with calf thymus histone H2A, the nematode protein shows five deletions, two insertions and 16 substitutions. Most of the changes occur in the N- and C-terminal regions of the molecule, whereas the central part covering the residues 21-120 is quite well conserved. The lysine residues 5, 8 and 10 were found to be partially acetylated.

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.

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

1972 ◽  
Vol 130 (2) ◽  
pp. 443-452 ◽  
Author(s):  
S. Doonan ◽  
H. J. Doonan ◽  
F. Riva ◽  
C. A. Vernon ◽  
J. M. Walker ◽  
...  
Keyword(s):  
Amino Acid ◽  
Primary Structure ◽  
Aspartate Aminotransferase ◽  
Heart Muscle ◽  
Science And Technology ◽  
Complex Mixture ◽  
Amino Acid Sequences ◽  
Tryptic Digestion ◽  
Amino Acid Residues ◽  
Lending Library

Peptides obtained by tryptic digestion of carboxymethylated and maleylated aspartate aminotransferase and of the aminoethylated enzyme were isolated and the complete amino acid sequences of most of them were determined. Digestion of the carboxymethylated protein with pepsin produced a complex mixture of peptides that allowed some overlapping of the tryptic peptides (Fig. 4); in addition, peptides were obtained that had not been found in either of the tryptic digests. From these studies about 400 amino acid residues were identified. Experimental details and confirmatory data for the results presented here are given in a supplementary paper that has been deposited as Supplementary Publication 50011 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. (1972) 126, 5.

scholarly journals The amino acid sequence of chymopapain from Carica papaya

1990 ◽  
Vol 266 (1) ◽  
pp. 75-81 ◽  
Author(s):  
D C Watson ◽  
M Yaguchi ◽  
K R Lynn
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Structural Similarity ◽  
Thiol Group ◽  
Exchange Chromatography ◽  
British Library ◽  
Amino Acid Residues ◽  
Main Paper ◽  
Paper Supplement ◽  
Mild Acid

Chymopapain is a polypeptide of 218 amino acid residues. It has considerable structural similarity with papain and papaya proteinase omega, including conservation of the catalytic site and of the disulphide bonding. Chymopapain is like papaya proteinase omega in carrying four extra residues between papain positions 168 and 169, but differs from both papaya proteinases in the composition of its S2 subsite, as well as in having a second thiol group, Cys-117. Some evidence for the amino acid sequence of chymopapain has been deposited as Supplementary Publication SUP 50153 (12 pages) at the British Library Document Supply Centre, Boston Spa., Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies may be obtained on the terms indicated in Biochem. J. (1990) 265, 5. The information comprises Supplement Tables 1-4, which contain, in order, amino acid compositions of peptides from tryptic, peptic, CNBr and mild acid cleavages, Supplement Fig. 1, showing re-fractionation of selected peaks from Fig. 2 of the main paper. Supplement Fig. 2, showing cation-exchange chromatography of the earliest-eluted peak of Fig. 3 of the main paper, Supplement Fig. 3, showing reverse-phase h.p.l.c. of the later-eluted peak from Fig. 3 of the main paper, and Supplement Fig. 4, showing the separation of peptides after mild acid hydrolysis of CNBr-cleavage fragment CB3.

N.M.R. studies of myelin basic protein. VI. Proton spectra in aqueous solutions of proteins from mammalian and avian species

1982 ◽  
Vol 35 (10) ◽  
pp. 1979 ◽  
Author(s):  
GL Mendz ◽  
WJ Moore ◽  
PR Carnegie
Keyword(s):  
Aqueous Solution ◽  
Primary Structure ◽  
Chemical Shifts ◽  
Side Chains ◽  
Amino Acid Residues ◽  
Difference Spectra ◽  
Effects Of Ph ◽  
Central Nervous Systems ◽  
Species Comparisons ◽  
Nuclear Overhauser

Myelin basic proteins from human, cow, pig, rabbit and chicken central nervous systems were studied in aqueous solution by proton n.m.r. at 400 MHz. Species comparisons and other techniques led to the assignment of resonances of 23 specific amino acid residues in the primary structure. Resonances from side chains of polar amino acids adjacent to aspartic residues could be assigned by anomalous effects of pH on the chemical shifts. The pK values of histidine side chains all fall in the range 6.0-6.9, and four specific histidine residues were assigned. The conformation of the protein in aqueous solution is that of an extended non-random polypeptide chain with regions of localized structure. Nuclear Overhauser difference spectra showed that a reverse turn similar to that previously suggested for an encephalitogenic nonapeptide isolated from the protein (guinea pig determinant) occurs also in the protein itself, thus supporting the concept of special low-energy conformations responsible for biological activity. Upfield chemical shifts of some side chain methyl groups from the central region of the primary structure suggest ring-current shifts due to higher-order structuring.

Comparative study of rye and thymus histones: amino acid analysis and tryptic fingerprinting

1977 ◽  
Vol 55 (7) ◽  
pp. 721-727 ◽  
Author(s):  
Paul Nadeau ◽  
Dominick Pallotta ◽  
Jean-G. Lafontaine
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Secale Cereale ◽  
Primary Structure ◽  
Amino Acid Analysis ◽  
General Pattern ◽  
The Other ◽  
Amino Acid Residues ◽  
Additional Segment ◽  
Similar Amino Acid

Amino acid composition and tryptic fingerprints of rye (Secale cereale) H1, H2B (PHI), and H2A (PHII) histones indicate the presence of major differences between these and the corresponding calf or rabbit fractions. In addition to variations for other amino acids, fraction H1 from rye contains twice as much arginine as the corresponding animal fraction; the plant H2B (PHI) and H2A (PHII) histones show lysine to arginine ratios greater than those of their animal counterparts. The tryptic maps of the same proteins appear to differ between plants and animals by the number and the general pattern of the peptides, as well as by the quantity and distribution of the arginine-containing peptides. Such results suggest the presence of differences in the primary structure of the calf and rye lysine-rich and moderately lysine-rich histones. Furthermore, the possibility is ruled out that each of these plant histones consists of an animal-like protein with an additional segment of 20–30 amino acid residues. On the other hand, the rye and calf arginine-rich fractions H3 and H4 show similar amino acid compositions and tryptic peptides maps.

scholarly journals Primary structure of the telopeptide and a portion of the helical domain of chicken type II procollagen as determined by DNA sequence analysis

1985 ◽  
Vol 229 (1) ◽  
pp. 189-196 ◽  
Author(s):  
F Deák ◽  
W S Argraves ◽  
I Kiss ◽  
K J Sparks ◽  
P F Goetinck
Keyword(s):  
Sequence Analysis ◽  
Dna Sequence ◽  
Primary Structure ◽  
Nucleotide Sequences ◽  
Dna Sequence Analysis ◽  
The Other ◽  
Cdna Clones ◽  
Type Ii ◽  
Lysine Residues ◽  
Replacement Site

A comparison of the nucleotide sequences of three new cDNA clones for chicken type II procollagen with the sequences of the other three types of chicken fibrillar procollagens reveals that the most conserved regions correlate with the positions of hydroxyproline, hydroxylysine, cysteine and lysine residues. On the basis of replacement-site-divergence calculations it is concluded that alpha 1(II) and alpha 1(I) procollagens diverged later than alpha 1(I) and alpha 2(I) procollagens.

scholarly journals Identification of the apparently essential lysine residues in phospholipase C (Bacillus cereus)

1981 ◽  
Vol 193 (3) ◽  
pp. 805-809
Author(s):  
B J Myrnes ◽  
C Little
Keyword(s):  
Amino Acid ◽  
Bacillus Cereus ◽  
Phospholipase C ◽  
Primary Structure ◽  
Lysine Residue ◽  
The Other ◽  
Proline Residue ◽  
Terminal Fragment ◽  
Lysine Residues ◽  
Essential Lysine Residues

Phospholipase C (Bacillus cereus) contains two apparently essential and very reactive lysine residues that may be labelled selectively by pyridoxal 5′-phosphate [Aurebekk & Little (1977) Biochem, J. 161, 159–165]. One of these lysine residues was found in the 25-amino acid N-terminal fragment liberated by CNBr digestion of the pyridoxal-labelled enzyme and identified as lysine-6. Two of the labelled peptides isolated from the chymotryptic digest of pyridoxal-labelled enzyme contained proline, suggesting that the other labelled lysine residue is situated in the same region of the primary structure as the single proline residue of the enzyme.

The Reaction of Chymotrypsin with 2,3-Butanedione Trimer

1975 ◽  
Vol 53 (3) ◽  
pp. 275-283 ◽  
Author(s):  
H. Fliss ◽  
N. M. Tozer ◽  
T. Viswanatha
Keyword(s):  
Amino Acid ◽  
Enzymatic Activity ◽  
Residual Activity ◽  
Amino Acid Residues ◽  
Lysine Residues ◽  
Arginine Residues ◽  
Chymotrypsin A

A method for the preparation of the trimer of 2,3-butanedione has been developed. The reaction of this trimer with chymotrypsin Aα was examined in the presence or absence of light. Under conditions of exclusion of light, modification of one to two arginine residues and of a similar number of lysine residues could be achieved without any loss of enzymatic activity. The trimer facilitated a rapid photoinactivation of the enzyme with little or no modification of the above amino acid residues. Such photoinactivation was not promoted by the monomer 2,3-butanedione. Enzyme irradiated in the presence of the trimer was found to react with proflavine and diisopropylfluorophosphate to an extent greater than that expected on the basis of residual activity present. Proflavine protected the enzyme from the trimer promoted photoinactivation.

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