High-sensitivity amino acid sequence determination of radioactive proteins made in vivo or in vitro

1982 ◽  
Vol 122 (2) ◽  
pp. 322-327 ◽  
Author(s):  
Masaru Ryoji ◽  
Akira Kaji
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
High Sensitivity ◽  
Sequence Determination ◽  
Made In

scholarly journals Primary Structure of Human Platelet Factor 4.

1977 ◽  
Author(s):  
F.J. Morgan ◽  
G.S. Begg ◽  
C.N. Chesterman
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Structural Information ◽  
Human Platelet ◽  
Specific Protein ◽  
Platelet Factor 4 ◽  
Platelet Factor ◽  
Tryptic Peptides

The amino acid sequence of human platelet factor 4 (PF4) has been studied. PF4 is a platelet specific protein with antiheparin activity, released from platelets as a proteoglycan complex, whose measurement may provide an important index of platelet activation both in vivo and in vitro. These studies were undertaken to characterize fully the PF4 molecule. PF4 is a stable tetramer, composed of identical subunits, each with a molecular weight based on the sequence studies of approx. 7,770. Each PF4 subunit contains 69 amino acids, including 4 half-cystine (# 10, 12, 36, 37), one tyrosine (# 59), 3 arginine and 8 lysine, but no methionine, phenylalanine or tryptophan residues. The basic residues are predominantly in the C-terminal region. The tryptic peptides were aligned after studies which included tryptic digestion of citraconylated RCM-PF4, and automated Edman degradation of RCM-PF4 and citraconylated tryptic peptides. No glycopeptides were detected. This structural information should enable clear distinction to be made between PF4 and other platelet proteins such as β thromboglobulin. The provisional amino acid sequence of each subunit is:Glu-Ala-Glu-Glu-Asp-Gly-Asp-Leu-Gln-Cys-Leu-Cys-Val-Lys-Thr-Thr-Ser-Gln-Val-Arg-Pro-Arg-His-Ile-Thr-Ser-Leu-Glu-Val-Ile-Lys-Ala-Gly-Pro-His-Cys-Cys-Pro-Thr-Ala-Gln-Ile-Leu-Ala-Thr-Leu-Lys-Asn-Gly-Arg-Lys-Ile-Pro-Leu-Asp-Leu-Gln-Ala-Tyr-Leu-Lys-Ile-Lys(Lys, Lys, Ser, Glx, Leu, Leu)

Partial amino acid sequence determination of Bovine Corneal Protein 54 K (BCP 54)

1990 ◽  
Vol 9 (8) ◽  
pp. 781-786 ◽  
Author(s):  
David L. Cooper ◽  
Edward W. Baptist ◽  
Jan Enghild ◽  
Howard Lee ◽  
Narayana Isola ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Sequence Determination ◽  
Partial Amino Acid Sequence

scholarly journals Mutagenesis of the Rns regulator of enterotoxigenic Escherichia coli reveals roles for a linker sequence and two helix–turn–helix motifs

Microbiology ◽  
2010 ◽  
Vol 156 (9) ◽  
pp. 2796-2806 ◽  
Author(s):  
Vivienne Mahon ◽  
Cyril J. Smyth ◽  
Stephen G. J. Smith
Keyword(s):  
Gene Expression ◽  
Escherichia Coli ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Protein A ◽  
Diarrhoeal Disease ◽  
Enterotoxigenic Escherichia Coli ◽  
Insertion Mutagenesis

The pathogenesis of diarrhoeal disease due to human enterotoxigenic Escherichia coli absolutely requires the expression of fimbriae. The expression of CS1 fimbriae is positively regulated by the AraC-like protein Rns. AraC-like proteins are DNA-binding proteins that typically contain two helix–turn–helix (HTH) motifs. A program of pentapeptide insertion mutagenesis of the Rns protein was performed, and this revealed that both HTH motifs are required by Rns to positively regulate CS1 fimbrial gene expression. Intriguingly, a pentapeptide insertion after amino acid C102 reduced the ability of Rns to transactivate CS1 fimbrial expression. The structure of Rns in this vicinity (NACRS) was predicted to be disordered and thus might act as a flexible linker. This hypothesis was confirmed by deletion of this amino acid sequence from the Rns protein; a truncated protein that lacked this sequence was no longer functional. Strikingly, this sequence could be functionally substituted in vivo and in vitro by a flexible seven amino acid sequence from another E. coli AraC-like protein RhaS. Our data indicate that HTH motifs and a flexible sequence are required by Rns for maximal activation of fimbrial gene expression.

scholarly journals Amino acid sequence determination of Ancrod, the thrombin-like α-fibrinogenase from the venom of Akistrodon rhodostoma

FEBS Letters ◽  
1992 ◽  
Vol 297 (3) ◽  
pp. 297-301 ◽  
Author(s):  
William Burkhart ◽  
Gardiner F.H. Smith ◽  
Jui-Lan Su ◽  
Indu Parikh ◽  
Harry LeVine
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Sequence Determination

scholarly journals The cDNA and derived amino acid sequence of porcine factor VIII

Blood ◽  
1996 ◽  
Vol 88 (11) ◽  
pp. 4209-4214 ◽  
Author(s):  
JF Healey ◽  
IM Lubin ◽  
P Lollar
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Factor Viii ◽  
Untranslated Region ◽  
Hemophilia A ◽  
Sequence Determination ◽  
C2 Domains ◽  
Protein Alignments ◽  
A2 Domain

The cDNA corresponding to 137 bp of the 5′ untranslated region, the signal peptide, and the A1, A3, C1, and C2 domains of porcine factor VIII (fVIII) have been cloned and sequenced. Along with previously determined sequences of the porcine fVIII B domain and the A2 domain, this completes the sequence determination of the cDNA corresponding to the translated protein. Alignments of the derived amino acid sequence of porcine fVIII with human and murine fVIII indicate that the A1, A2, A3, C1, and C2 domains are more conserved than the B domains or the proteolytic cleavage peptides corresponding to residues 337–372 and 1649–1689. The knowledge of the porcine fVIII cDNA may be useful to understand functional and immunological differences between human and porcine fVIII and may lead to improved fVIII replacement products for hemophilia. A patients through the development of recombinant porcine fVIII or hybrid human/porcine fVIII derivatives.

Precursor of Rat Liver α2u-Globulin: Partial Amino Acid Sequence Determination of Its Signal Peptide1

1981 ◽  
Vol 90 (6) ◽  
pp. 1833-1836 ◽  
Author(s):  
Yukio IKEHARA ◽  
Kimimitsu ODA ◽  
Melvin G. ROSENFELD ◽  
Shoshana BAR-NUN ◽  
Gert KREIBICH
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Rat Liver ◽  
Sequence Determination ◽  
Partial Amino Acid Sequence
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