The ADP-ribosylating thermozyme from Sulfolobus solfataricus is a DING protein

2009 ◽  
Vol 390 (1) ◽  
Author(s):  
Antimo Di Maro ◽  
Anna De Maio ◽  
Sabrina Castellano ◽  
Augusto Parente ◽  
Benedetta Farina ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Sulfolobus Solfataricus ◽  
Terminal Region ◽  
High Similarity ◽  
Partial Amino Acid Sequence ◽  
Tryptic Peptides ◽  
Ding Protein ◽  
N Terminus

Abstract The partial amino acid sequence of the sulfolobal thermoprotein biochemically characterized as poly(ADP-ribose)polymerase-like enzyme overlaps those of DING proteins. This group of proteins, widely occurring in animals, plants and eubacteria, shows a characteristic and highly conserved N-terminus, DINGGGATL. The sequence of the N-terminal region and of the analyzed tryptic peptides of the sulfolobal thermozyme shows a high similarity with most of the DING proteins from databases. This is the first example of a DING protein from a sulfolobal source.

scholarly journals The amino acid sequence of the α chain of the major haemoglobin of the rat (Rattus norvegicus)

1975 ◽  
Vol 149 (1) ◽  
pp. 259-269 ◽  
Author(s):  
C G Chua ◽  
R W Carrell ◽  
B H Howard
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Rattus Norvegicus ◽  
Peptide Mapping ◽  
Cysteine Residue ◽  
British Library ◽  
Peptide Fragments ◽  
Partial Amino Acid Sequence ◽  
Tryptic Peptides ◽  
Α Chain

1. A partial amino acid sequence of the α chain from the rat (Wistar, Rattus norvegicus) major haemoglobin is reported. The soluble tryptic peptides prepared from aminoethylated α-globin were separated by peptide ‘mapping’. Sequencing of the tryptic peptides was carried out by the dansyl-Edman method and by the overlapping of smaller peptide fragments derived from secondary enzymic digestion. The insoluble ‘core’ peptides were further digested with chymotrypsin, thermolysin and pepsin to give smaller soluble peptides for sequencing. The tryptic peptides were ordered on the basis of their homology with the corresponding peptides of human α chain. 2. The proposed sequence is compared with that obtained by using an automated sequencer [Garrick et al. (1975) Biochem. J.149, 245-258]. The differences in sequence resulting from the two methods are discussed. 3. It is suggested that the externally situated cysteine (residue 13) is responsible for the observed inhibition of crystallization of rat haemoglobin at alkaline pH. 4. Detailed evidence for the sequence has been deposited as Supplementary Publication SUP 50047 (9 pages) at the British Library (Linding Division), Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from which copies can be obtained on the terms given in Biochem. J. (1975) 145, 5.

Amino acid sequence of the N-terminus and selected tryptic peptides of the active subunit of human plasma carboxypeptidase N: comparison with other carboxypeptidases

1988 ◽  
Vol 154 (3) ◽  
pp. 1323-1329 ◽  
Author(s):  
Randal A. Skidgel ◽  
Carl D. Bennett ◽  
James W. Schilling ◽  
Fulong Tan ◽  
Deepthi K. Weerasinghe ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Human Plasma ◽  
Tryptic Peptides ◽  
N Terminus ◽  
Carboxypeptidase N

Partial amino acid sequence of some tryptic peptides of the alpha1 chain of hemoglobin

Life Sciences ◽  
1972 ◽  
Vol 11 (18) ◽  
pp. 895-899 ◽  
Author(s):  
Radim Brdička ◽  
Adriana Massa ◽  
Salvatore Carta ◽  
Leonardo Tentori ◽  
Gerolamo Vivaldi
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Partial Amino Acid Sequence ◽  
Tryptic Peptides

scholarly journals Partial amino acid sequence of rat pre-prolactin

1977 ◽  
Vol 161 (1) ◽  
pp. 189-192 ◽  
Author(s):  
R A Maurer ◽  
J Gorski ◽  
D J McKean
Keyword(s):  
Amino Acid ◽  
Sequence Analysis ◽  
Amino Acid Sequence ◽  
Cysteine Residue ◽  
Amino Acid Residues ◽  
Partial Amino Acid Sequence ◽  
Considerable Similarity ◽  
Rat Pituitary ◽  
N Terminus ◽  
Methionine Residues

Rat pituitary mRNA was used to direct the cell-free synthesis of pre-prolactin labelled with [4,5-3H]leucine and either [35S] methioninc or [35S] cystine. Sequence analysis of the labelled protein indicates that pre-prolactin has 29 amino acid residues joined to the N-terminus of the prolactin sequence. Leucine residues were found at positions 13, 14, 15, 16, 21 and 22, methionine residues at positions 1, 17 and 18, and a cysteine residue at position 24 of the precursor sequence, and this partial sequence shows considerable similarity with other precursors that have been sequenced.

N-terminal residues in murine P-selectin glycoprotein ligand-1 required for binding to murine P-selectin

Blood ◽  
2003 ◽  
Vol 101 (2) ◽  
pp. 552-559 ◽  
Author(s):  
Lijun Xia ◽  
Vishwanath Ramachandran ◽  
J. Michael McDaniel ◽  
Kiem N. Nguyen ◽  
Richard D. Cummings ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Chinese Hamster Ovary ◽  
Chinese Hamster Ovary Cells ◽  
Chinese Hamster ◽  
Fluid Phase ◽  
Terminal Region ◽  
Wild Type ◽  
Ovary Cells ◽  
N Terminus

P-selectin binds to the N-terminal region of human P-selectin glycoprotein ligand-1 (PSGL-1). For optimal binding, this region requires sulfation on 3 tyrosines and specific core-2O-glycosylation on a threonine. P-selectin is also thought to bind to the N terminus of murine PSGL-1, although it has a very different amino acid sequence than human PSGL-1. Murine PSGL-1 has potential sites for sulfation at Tyr13 and Tyr15 and for O-glycosylation at Thr14 and Thr17. We expressed murine PSGL-1 or constructs with substitutions of these residues in transfected Chinese hamster ovary cells that coexpressed the glycosyltransferases required for binding to P-selectin. The cells were assayed for binding to fluid-phase P-selectin and for tethering and rolling on P-selectin under flow. In both assays, substitution of Tyr13 or Thr17 markedly diminished, but did not eliminate, binding to P-selectin. In contrast, substitution of Tyr15 or Thr14 did not affect binding. Substitution of all 4 residues eliminated binding. Treatment of cells with chlorate, an inhibitor of sulfation, markedly reduced binding of wild-type PSGL-1 to P-selectin but did not further decrease binding of PSGL-1 with substitutions of both tyrosines. These data suggest that sulfation of Tyr13 andO-glycosylation of Thr17 are necessary for murine PSGL-1 to bind optimally to P-selectin. Because it uses only one tyrosine, murine PSGL-1 may rely more on other peptide components andO-glycosylation to bind to P-selectin than does human PSGL-1.

scholarly journals Partial amino acid sequence in the N-terminal region of an anti-pneumococcal immunoglobulin heavy chain of allotype a2

1974 ◽  
Vol 139 (1) ◽  
pp. 281-283 ◽  
Author(s):  
Jean-Claude Jaton ◽  
Joseph Haimovich
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Heavy Chain ◽  
Immunoglobulin Heavy Chain ◽  
Amino Acid Sequences ◽  
Terminal Region ◽  
Sequence Variability ◽  
Rabbit Antibody ◽  
Partial Amino Acid Sequence ◽  
Heavy Chains

The amino acid sequence of the N-terminal 48 residues of the heavy chain derived from a homogeneous rabbit antibody to type III pneumococci is described. This chain of allotype a2 is compared with other rabbit heavy chains of allotypes a1, a2 and a3. Within the N-terminal 25 positions, two chains which carry the same allotype a2 possess identical amino acid sequences, but differ markedly from heavy chains of allotypes a1 and a3. Sequence variability is observed in residues 26–27 and 30–34, but not in residues 35–48.

Peptide vaccine against canine parvovirus: identification of two neutralization subsites in the N terminus of VP2 and optimization of the amino acid sequence.

1995 ◽  
Vol 69 (11) ◽  
pp. 7274-7277 ◽  
Author(s):  
J I Casal ◽  
J P Langeveld ◽  
E Cortés ◽  
W W Schaaper ◽  
E van Dijk ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Peptide Vaccine ◽  
Canine Parvovirus ◽  
N Terminus

C-Terminal amino acid sequence of chicken pepsinogen and its homology with sequences of other acid proteases

1980 ◽  
Vol 45 (4) ◽  
pp. 1144-1154 ◽  
Author(s):  
Miroslav Baudyš ◽  
Helena Keilová ◽  
Vladimír Kostka
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
The Other ◽  
Terminal Sequence ◽  
Terminal Part ◽  
Terminal Amino Acid ◽  
Tryptic Peptides ◽  
Terminal Amino ◽  
High Degree ◽  
Terminal Amino Acid Sequence

To determine the primary structure of the C-terminal part of the molecule of chicken pepsinogen the tryptic, chymotryptic and thermolytic digest of the protein were investigated and peptides derived from this region were sought. These peptides permitted the following 21-residue C-terminal sequence to be determined: ...Ile-Arg-Glu-Tyr-Tyr-Val-Ile-Phe-Asp-Arg-Ala-Asn-Asn-Lys-Val-Gly-Leu-Ser-Pro-Leu-Ser.COOH. A comparison of this structure with the C-terminal sequential regions of the other acid proteases shows a high degree of homology between chicken pepsinogen and these proteases (e.g., the degree of homology with respect to hog pepsinogen and calf prochymosin is about 66%). Additional tryptic peptides, derived from the N-terminal part of the zymogen molecule whose amino acid sequence has been reported before, were also obtained in this study. This sequence was extended by two residues using an overlapping peptide. An ancillary result of this study was the isolation of tryptic peptides derived from other regions of the zymogen molecule.

Sign in / Sign up

Export Citation Format

Share Document