N- terminal sequence of moderately toxic phospholipase a from Vipera ammodytes venom

SummaryWith an immobilized synthetic pentapeptide GlyProArgProLys comprising the N-terminal sequence GlyProArg of the α-chain of fibrin, a new affinity method for the quantitative isolation of fibrinogen out of anticoagulated plasma was developed. The method proved to be superior to all known isolation methods in respect to ease of use and yield, since fibrinogen could be isolated in one step out of plasma with a recovery of more than 95% when compared to the immunologically measurable amounts of fibrinogen. Moreover the amounts of contaminating proteins such as fibronectin, factor XIII or plasminogen were negligible and the purity of the isolated fibrinogen was higher than 95% as measured by polyacrylamide gel electrophoresis. The clottability was 90% and more. Another advantage of this affinity purification method is the possibility to isolate fibrinogen quantitatively out of small plasma samples (<5 ml). Further, abnormal fibrinogen molecules, provided their complementary binding site for GlyProArg is preserved, may also be quantitatively isolated independent of any solubility differences as compared to normal fibrinogen. In addition fibrin(ogcn) fragments originating from plasmic digestion can be separated on the basis of their affinity to GlyProArg. The described affinity gel can be used more than 50 times without any loss of capacity.

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Faculty Opinions recommendation of The unique N-terminal sequence of the BKCa channel α-subunit determines its modulation by β-subunits.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.727845840.793553031 ◽

2018 ◽

Author(s):

Annette Dolphin

Keyword(s):

Bkca Channel ◽

Terminal Sequence ◽

Α Subunit

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Vipera ammodytes: Aram Agasyan, Aziz Avci, Boris Tuniyev, Jelka Crnobrnja Isailovic, Petros Lymberakis, Claes Andrén, Dan Cogalniceanu, John Wilkinson, Natalia Ananjeva, Nazan Üzüm, Nikolai Orlov, Richard Podloucky, Sako Tuniyev, Uğur Kaya, Roberto Sindaco, Wolfgang Böhme, Petros Lymberakis, Rastko Ajtic, Varol Tok, Ismail H. Ugurtas, Murat Sevinç, Ljiljana Tomović, Pierre-André Crochet, Idriz Haxhiu, Ulrich Joger, Bogoljub Sterijovski, Göran Nilson, Dušan Jelić

IUCN Red List of Threatened Species ◽

10.2305/iucn.uk.2009.rlts.t62255a12584303.en ◽

2008 ◽

Author(s):

Keyword(s):

Vipera Ammodytes

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

Collection of Czechoslovak Chemical Communications ◽

10.1135/cccc19801144 ◽

1980 ◽

Vol 45 (4) ◽

pp. 1144-1154 ◽

Cited By ~ 3

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.

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The melanocyte stimulating activity of N-nitroso-2-chloroethyl-carbamoyl derivatives of α-melanotropin fragments

Collection of Czechoslovak Chemical Communications ◽

10.1135/cccc19882574 ◽

1988 ◽

Vol 53 (11) ◽

pp. 2574-2582 ◽

Cited By ~ 5

Author(s):

Hedvig Medzihradszky-Schweiger ◽

Helga Süli-Vargha ◽

József Bódi ◽

Kálmán Medzihradszky

Keyword(s):

Biological Activity ◽

Active Site ◽

Frog Skin ◽

Terminal Sequence ◽

Subsequent Reaction ◽

Affinity Labels ◽

Derivatives Of

A number of N-nitroso-2-chloroethyl-carbamoyl (Q(NO)) derivatives of α-melanotropin fragments have been synthesized and their effect on the frog skin melanocytes studied. Peptides substituted in this way possess the biological activity of the parent compounds, indicating that they preserved their receptor recognizing ability. These compounds can therefore serve as affinity labels. Some of these derivatives, related to the C-terminal sequence of α-melanotropin show prolonged darkening reaction, which does not influence the subsequent reaction of melanocytes with α-melanotropin. The Q(NO)-derivative of a fragment derived from the classical active site of the hormone shows, however, inhibition of the effect of α-melanotropin. It can be concluded that the latter peptide acts through the melanotropin receptor, while others, related to the C-terminal sequence of the hormone through another mechanism.

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