Specifities of Rabbit Antisera to Multiple Antigen (MAP) Peptides

1995 ◽  
Vol 50 (9-10) ◽  
pp. 735-738
Author(s):  
Alberto Chersi ◽  
Francesca di Modugno ◽  
Giuliana Falasca
Keyword(s):  
Immune Response ◽  
Amino Acid ◽  
Amino Acid Residues ◽  
The Third ◽  
Multiple Antigen ◽  
Multiple Antigen Peptides

Abstract Two multiple antigen peptides consisting of 6 and 7 amino acid residues, respectively, plus a 12-residue fragment, used as a control, all linked to a polylysine core, were used as immunogens in rabbits in order to obtain an immune response. Rabbit antisera against such polymers were then tested in ELISA against a panel of antigens in order to analyze the specificites of the resulting antibodies. The responses were different for all three immunogens, being partially or totally directed, for two of the three compounds, including the 12-residue control MAP peptide, against the polylysyl core, which is considered as non immunogenic. The third MAP polymer was practically unable to elicit an immune response

The power of the force: mechano-physiology of the giant titin

2018 ◽  
Vol 2 (5) ◽  
pp. 681-686 ◽  
Author(s):  
Jaime Andrés Rivas-Pardo
Keyword(s):  
Amino Acid ◽  
Human Body ◽  
Actin Filaments ◽  
Polypeptide Chain ◽  
Single Gene ◽  
The Other ◽  
Amino Acid Residues ◽  
The Third ◽  
Single Polypeptide Chain ◽  
Single Polypeptide

Titin — the largest protein in the human body — spans half of the muscle sarcomere from the Z-disk to the M-band through a single polypeptide chain. More than 30 000 amino acid residues coded from a single gene (TTN, in humans Q8WZ42) form a long filamentous protein organized in individual globular domains concatenated in tandem. Owing to its location and close interaction with the other muscle filaments, titin is considered the third filament of muscle, after the thick-myosin and the thin-actin filaments.

scholarly journals Characterization of the Phd Repressor-Antitoxin Boundary

2005 ◽  
Vol 187 (2) ◽  
pp. 765-770 ◽  
Author(s):  
James Estle McKinley ◽  
Roy David Magnuson
Keyword(s):  
Amino Acid ◽  
Point Mutations ◽  
Modular Organization ◽  
Amino Acid Residues ◽  
The Third ◽  
Linear Sequence ◽  
C Terminus ◽  
Overlapping Sets ◽  
Repressor Activity

ABSTRACT The P1 plasmid addiction operon (a classic toxin-antitoxin system) encodes Phd, an unstable 73-amino-acid repressor-antitoxin protein, and Doc, a stable toxin. It was previously shown by deletion analysis that the N terminus of Phd was required for repressor activity and that the C terminus was required for antitoxin activity. Since only a quarter of the protein or less was required for both activities, it was hypothesized that Phd might have a modular organization. To further test the modular hypothesis, we constructed and characterized a set of 30 point mutations in the third and fourth quarters of Phd. Four mutations (PhdA36H, V37A, I38A, and F44A) had major defects in repressor activity. Five mutations (PhdD53A, D53R, E55A, F56A, and F60A) had major defects in antitoxin activity. As predicted by the modular hypothesis, point mutations affecting each activity belonged to disjoint, rather than overlapping, sets and were separated rather than interspersed within the linear sequence. A final deletion experiment demonstrated that the C-terminal 24 amino acid residues of Phd (preceded by a methionine) retained full antitoxin activity.

scholarly journals Different epitope structures select distinct mutant forms of an antibody variable region for expression during the immune response.

1991 ◽  
Vol 173 (3) ◽  
pp. 665-672 ◽  
Author(s):  
S Fish ◽  
M Fleming ◽  
J Sharon ◽  
T Manser
Keyword(s):  
Immune Response ◽  
Amino Acid ◽  
Somatic Mutation ◽  
Amino Acid Substitution ◽  
Variable Region ◽  
Single Amino Acid ◽  
Amino Acid Residues ◽  
V Region ◽  
Mutant Forms ◽  
Selection Of

Antibody variable (V) regions that initially differ from one another by only single amino acid residues at VH-D and D-JH segment junctions (termed canonical V regions) can be elicited in strain A/J mice by three different haptens. Among such V regions an amino acid substitution due to somatic mutation is recurrently observed at VH CDR2 position 58, regardless of which of these haptens is used for immunization. This substitution confers upon a canonical V region a generic increase in affinity for all the haptens. Conversely, the type of amino acid substitution at VH position 59 resulting from somatic mutation that is recurrently observed among such V regions changes with the eliciting hapten, in a manner that correlates directly with the cognate affinity increases (or decreases) for hapten conferred by the observed substitutions. This small subregion of VH CDR2 therefore plays a major role in determining both affinity and specificity for antigen. The data confirm that affinity for antigen is of pivotal importance in determining the degree of selection of different mutant forms of a V region. Moreover, during an immune response a sufficiently diverse mutant repertoire can be generated from a single canonical V region to allow adaptation to increase affinity for three different epitopes.

scholarly journals Amino acid residues in the third alpha-helix of growth hormone involved in growth promoting activity.

1995 ◽  
Vol 9 (3) ◽  
pp. 292-302
Author(s):  
W Y Chen ◽  
N Y Chen ◽  
J Yun ◽  
D C Wight ◽  
X Z Wang ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Amino Acid ◽  
Alpha Helix ◽  
Amino Acid Residues ◽  
The Third ◽  
Growth Promoting

scholarly journals ANTIGENICITY OF POLYPEPTIDES (POLY ALPHA AMINO ACIDS)

1965 ◽  
Vol 122 (4) ◽  
pp. 665-671 ◽  
Author(s):  
Paul Pinchuck ◽  
Paul H. Maurer
Keyword(s):  
Amino Acids ◽  
Immune Response ◽  
Amino Acid ◽  
Immune Responses ◽  
Random Sequence ◽  
Inbred Strains ◽  
The Third ◽  
Swiss Mice

The response of mice to synthetic linear polypeptides of known composition but random sequence has been studied. Neither Swiss mice nor a number of inbred strains could respond to copolymers of only 2 amino acids (G60L40, G60A40, G90T10). Upon introduction of as little as 4 mole per cent of a third amino acid, good immune responses were obtained, regardless of the nature of the third amino acid. The level of the immune response to a series of glu-lys-ala polymers increased with increasing alanine content of the polymer.

scholarly journals Key Amino Acid Residues within the Third Membrane Domains of NR1 and NR2 Subunits Contribute to the Regulation of the Surface Delivery ofN-methyl-d-aspartate Receptors

2012 ◽  
Vol 287 (31) ◽  
pp. 26423-26434 ◽  
Author(s):  
Martina Kaniakova ◽  
Barbora Krausova ◽  
Vojtech Vyklicky ◽  
Miloslav Korinek ◽  
Katarina Lichnerova ◽  
...  
Keyword(s):  
Amino Acid ◽  
Membrane Domains ◽  
Amino Acid Residues ◽  
The Third ◽  
Nr2 Subunits

scholarly journals Phosphorylase kinase phosphorylation of skeletal-muscle troponin T

1980 ◽  
Vol 191 (3) ◽  
pp. 851-854 ◽  
Author(s):  
V V Risnik ◽  
A B Dobrovolskii ◽  
N B Gusev ◽  
S E Severin
Keyword(s):  
Skeletal Muscle ◽  
Amino Acid ◽  
Troponin T ◽  
Rabbit Skeletal Muscle ◽  
Phosphorylase Kinase ◽  
Amino Acid Residues ◽  
Standard Preparation ◽  
The Third ◽  
Original Preparation ◽  
Kinase Phosphorylation

Rabbit skeletal-muscle troponin T was phosphorylated by a standard preparation of phosphorylase kinase [Cohen (1973) Eur. J. Biochem. 34, 1–14] and by fractions obtained after chromatography of phosphorylase kinase on phosphocellulose. The original preparation of phosphorylase kinase phosphorylated at least two sites, one of which was serine-1. The second and probably the third sites were presumably located in the peptide flanked by amino-acid residues 147 and 161 of troponin T. Fractions of phosphorylase kinase was adsorbed on phosphocellulose phosphorylated only the second site. Tightly adsorbed fractions possessed high troponin T kinase and phosvitin kinase activities and phosphorylated only serine-1 of troponin T. The results suggest that standard preparations of phosphorylase kinase are contaminated by troponin T kinase, which can phosphorylate serine-1 of troponin T.

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