scholarly journals Chemical Characterization of a Non-Covalently Linked Peptide from Plakalbumin

1969 ◽  
Vol 22 (1) ◽  
pp. 239 ◽  
Author(s):  
R Sleigh ◽  
R Hosken MB Smith ◽  
EOP Thompson
Keyword(s):  
Chemical Characterization ◽  
Protein Component ◽  
Terminal Portion ◽  
Terminal Sequence ◽  
Covalently Linked

A 33�residue peptide isolated from plakalbumin by dissociation with urea at pH 3 is shown to be derived from the a-terminal portion of ovalbumin. The yield of proline obtained on hydrazinolysis was the same as that from ovalbumin, whereas proline was not liberated from the protein component. The N�terminal sequence of this peptide was determined by the Edman degradative procedure to be Ser. V al.Ser .Glu.Glu.Phe.Arg.Ala.Asp.

scholarly journals Characterization of the 70 kDa polypeptide of the Na/Ca exchanger

1999 ◽  
Vol 338 (1) ◽  
pp. 139-145 ◽  
Author(s):  
Rami I. SABA ◽  
Alex BOLLEN ◽  
André HERCHUELZ
Keyword(s):  
Wild Type ◽  
Terminal Portion ◽  
Terminal Sequence ◽  
Protein Ratio ◽  
Reducing Conditions ◽  
Sds Page ◽  
Cloned Bovine ◽  
Sarcolemmal Vesicles ◽  
Exchange Activity

The Na/Ca exchanger is associated with 160, 120 and 70 kDa polypeptides whose nature is poorly understood. We have purified and characterized the Na/Ca exchanger from bovine cardiac sarcolemmal vesicles (SLVs) by using ion-exchange and affinity chromatographies. The Na/Ca exchanger-enriched fraction was reconstituted into asolectin liposomes [lipid to protein ratio 10:1 (w/w)] that showed Na/Ca exchange activity. Under non-reducing conditions, SDS/PAGE showed a single 70 kDa polypeptide, which was further characterized by immunoblots with different antibodies: SWant, raised against the purified exchanger protein; NH2-terminus, residues 1–21; NCX1, residues 393–406; and Exon F, residues 622–644. Immunoblots under reducing conditions with SWant, NH2-terminus and NCX1 showed three bands migrating at 160, 120 and 70 kDa for SLV preparations, whereas Exon F reacted only with the 160 and 120 kDa bands. Under non-reducing conditions, immunoblots with purified reconstituted Na/Ca exchanger showed a single band at 70 kDa reacting with SWant, NH2-terminus and NCX1 but not with Exon F. We conclude that the 70 kDa protein is associated with Na/Ca exchange activity, has the same N-terminal sequence as the cloned bovine cardiac exchanger, and has its length decreased by at least 35% from its C-terminal portion as compared with that of the wild-type exchanger.

scholarly journals Toxic peptides and genes encoding toxin γ of the Brazilian scorpions Tityus bahiensis and Tityus stigmurus

1996 ◽  
Vol 313 (3) ◽  
pp. 753-760 ◽  
Author(s):  
Baltazar BECERRIL ◽  
Miguel CORONA ◽  
Fredy I. V. CORONAS ◽  
Fernando ZAMUDIO ◽  
Emma S. CALDERONARANDA ◽  
...  
Keyword(s):  
Chemical Characterization ◽  
Large Degree ◽  
Cross Reactivity ◽  
Terminal Sequence ◽  
Cdna Sequences ◽  
Genes Encoding ◽  
Tityus Serrulatus ◽  
Toxic Peptides ◽  
Degree Of Similarity

Seven toxic peptides from the venom of Tityus bahiensis and Tityus stigmurus were isolated and sequenced, five of them to completion. The most abundant peptide from each of these two species of scorpion was 95% identical with that of toxin γ from the venom of Tityus serrulatus. They were consequently named γ-b and γ-st respectively. The genes encoding these new γ-like peptides were cloned and sequenced by utilizing oligonucleotides synthesized according to known cDNA sequences of toxin γ, and amplified by PCR on templates of DNA purified from both T. bahiensis and T. stigmurus. They contain an intron of approx. 470 bp. Possible mechanisms of processing and expressing these peptides are discussed, in view of the fact that glycine is the first residue of the N-terminal sequence of T. stigmurus, whereas lysine is the residue at position 1 of toxin γ from T. serrulatus and T. bahiensis. In addition, chemical characterization of the less abundant toxic peptides showed the presence of at least four distinct families of peptides in all three species of the genus Tityus studied. There is a large degree of similarity among peptides from different venoms of the same family. By using specific horse and rabbit antisera, the venoms of T. bahiensis, T. serrulatus and T. stigmurus were compared. They showed an extended degree of cross-reactivity. Thus these three species of scorpion have similar toxic components, the genes of which are similarly organized, processed and expressed.

The Immuno-Electron Microscopic Localization of the Mo-Fe Protein Component of Nitrogenase in Cells of Azotobacter Vinelandii

1973 ◽  
Vol 31 ◽  
pp. 574-575
Author(s):  
J. T. Stasny ◽  
R. C. Burns ◽  
R. W. F. Hardy
Keyword(s):  
Cellular Localization ◽  
Direct Evidence ◽  
Azotobacter Vinelandii ◽  
Intracellular Localization ◽  
Protein Component ◽  
Electron Microscopic ◽  
Thin Sections ◽  
Fe Protein ◽  
Intracytoplasmic Membranes

Structure-functlon studies of biological N2-fixation have correlated the presence of the enzyme nitrogenase with increased numbers of intracytoplasmic membranes in Azotobacter. However no direct evidence has been provided for the internal cellular localization of any nitrogenase. Recent advances concerned with the crystallizatiorTand the electron microscopic characterization of the Mo-Fe protein component of Azotobacter nitrogenase, prompted the use of this purified protein to obtain antibodies (Ab) to be conjugated to electron dense markers for the intracellular localization of the protein by electron microscopy. The present study describes the use of ferritin conjugated to goat antitMo-Fe protein immunoglobulin (IgG) and the observations following its topical application to thin sections of N2-grown Azotobacter.

Olfactory and Chemical Characterization of Indoor Air-Towards a Psychophysical Model for Air Quality

1981 ◽  
Author(s):  
Birgitta Berglund ◽  
Ulf Berglund ◽  
Thomas Lindvall ◽  
Helene Nicander-Bredberg
Keyword(s):  
Air Quality ◽  
Indoor Air ◽  
Chemical Characterization

PURIFICATION AND PARTIAL CHEMICAL CHARACTERIZATION OF SHEEP NEUROPHYSIN

1973 ◽  
Vol 74 (2) ◽  
pp. 226-236 ◽  
Author(s):  
Michel Chrétien ◽  
Claude Gilardeau
Keyword(s):  
Amino Acid ◽  
Polyacrylamide Gel Electrophoresis ◽  
Chemical Characterization ◽  
Terminal Amino Acid ◽  
Amino Acid Determination ◽  
Pituitary Glands ◽  
Terminal Amino ◽  
Partial Chemical ◽  
Acid Determination

ABSTRACT A protein isolated from ovine pituitary glands has been purified, and its homogeneity assessed by NH2- and COOH-terminal amino acid determination, ultracentrifugation studies, and polyacrylamide gel electrophoresis after carboxymethylation. Its chemical and immunochemical properties are closely similar to those of beef and pork neurophysins, less similar to those of human neurophysins. It contains no tryptophan (like other neurophysins) or histidine (like all except bovine neurophysin-I and human neurophysins). It has alanine at the NH2-terminus and valine at the COOH-terminus. Its amino acid composition is similar to, but not identical with those of porcine and bovine neurophysins.

Laboratory Methods for the Physico-Chemical Characterization of Recombinant Allergens as Reference Standards

Alergologia ◽  
2020 ◽  
Vol 1 (4) ◽  
pp. 7
Author(s):  
Mariana Vieru ◽  
Florin-Dan Popescu ◽  
Laura Haidar ◽  
Carmen Bunu-Panaitescu
Keyword(s):  
Chemical Characterization ◽  
Reference Standards ◽  
Recombinant Allergens ◽  
Laboratory Methods ◽  
Physico Chemical
Sign in / Sign up

Export Citation Format

Share Document