Unequal importance of different polypeptide chains for the determination of antibody specificity in bovine anti-dinitrophenyl antibodies

1965 ◽  
Vol 30 (9) ◽  
pp. 3153-3163 ◽  
Author(s):  
O. Kotýnek ◽  
F. Franěk
Keyword(s):  
Antibody Specificity ◽  
Polypeptide Chains

The Italian Quality Control Scheme for Crossmatching Procedures and HLA Sera Screening: The 2002 Pilot Study

2005 ◽  
Vol 129 (11) ◽  
pp. 1470-1475
Author(s):  
Raffaele Conca ◽  
Loredana Praticò-Barbato ◽  
Anna Maria Dall'Omo ◽  
Antonio Amoroso
Keyword(s):  
Quality Control ◽  
Serum Antibody ◽  
Hla Typing ◽  
European Federation ◽  
Antibody Specificity ◽  
Control Scheme ◽  
National Quality ◽  
Transplant Immunology ◽  
Quality Control Scheme

Abstract Context.—The first national quality control (QC) program of histocompatibility serum testing was performed in Italy in 2002. Objective.—To monitor the performance of HLA typing laboratories while meeting the accreditation requirements of the European Federation for Immunogenetics (EFI), which require HLA typing laboratories to participate in external QC of their crossmatch and antibody analyses. Design.—The Turin Transplant Immunology Service was asked to organize a QC survey of 17 HLA typing laboratories in Italy. Each laboratory received 12 serum specimens and 6 blood samples and was required to perform 36 crossmatches and 12 serum antibody specificity determinations. Settings.—Data of participating centers were compared to establish whether EFI requirements were satisfied. Results.—In crossmatch analysis, the results of 32 of 36 crossmatches reached the 75% consensus target, with all the participating laboratories meeting the standards of the EFI. In antibody analysis, only 7 of 17 laboratories met the EFI standards. Conclusion.—The first Italian QC program shows that the participating laboratories obtained consistent results in crossmatching, whereas the results were less satisfactory in the determination of serum antibody specificity, where consensus was reached only with monospecific sera and antibody-negative samples.

Address of the President Lord Todd at the anniversary meeting, 30 November 1976

1977 ◽  
Vol 352 (1671) ◽  
pp. 451-462
Keyword(s):  
Protein Interactions ◽  
Complex Analysis ◽  
Organic Molecules ◽  
Heavy Atom ◽  
Vitamin B ◽  
Protein Protein Interactions ◽  
X Ray Crystallography ◽  
Polypeptide Chains ◽  
Complex Organic

The Copley Medal is awarded to Professor Dorothy M. C. Hodgkin, O. M., F. R. S. Professor Dorothy Hodgkin is distinguished for her research on the structure of complex organic molecules by the method of X-ray crystallography. She was among the first to appreciate the importance of heavy-atom phase-determining methods and these she used to effect the first complete determination of the stereochemistry of a sterol derivative in her analysis of cholesteryl iodide. The same powerful method of analysis and in particular her extraordinary gift of being able to interpret correctly the complex, partially resolved and often misleading electron density patterns that are first obtained, have been responsible for her success in elucidating the structures of many other important natural products, especially penicillin and vitamin B 12 . This last is by far the most beautiful and complex analysis which has yet been completed in this field and it is of fundamental importance to chemical science. In recent years Professor Hodgkin’s main interest has been devoted to the structure of insulin, on which she has been working on and off since 1935. Carried out with characteristic precision, this work has become a mine of stereochemical information relating to contacts between polypeptide chains and is of great significance for our interpretation of protein-protein interactions.

Studies on the site of addition of sialic acid and glucosamine to rat α1-acid glycoprotein

1977 ◽  
Vol 55 (4) ◽  
pp. 408-414 ◽  
Author(s):  
J. C. Jamieson
Keyword(s):  
Endoplasmic Reticulum ◽  
Sialic Acid ◽  
Rat Liver ◽  
Golgi Complex ◽  
Smooth Endoplasmic Reticulum ◽  
Main Site ◽  
Acid Glycoprotein ◽  
Membrane Bound ◽  
Polypeptide Chains

Ultrasonic extracts of rough and smooth endoplasmic reticulum fractions and Golgi fractions from rat liver were examined by immunoelectrophoresis using antiserum to α1-acid glycoprotein. Rough endoplasmic reticulum fractions contained only sialic acid free α1-acid glycoprotein, whereas smooth endoplasmic reticulum and Golgi fractions also contained sialic acid containing α1-acid glycoprotein. Determination of the sialic acid contents of immune precipitates isolated from the extracts suggested that the Golgi complex was the main site of addition of sialic acid to α1-acid glycoprotein. Immunological studies on puromycin extracts of polyribosomes showed that polypeptide chains of α1-acid glycoprotein and albumin were assembled mainly on membrane-bound polyribosomes. Evidence is presented from incorporation studies with labelled leucine and glucosamine that initial glycosylation of α1-acid glycoprotein occurs mainly or entirely after release of nascent polypeptide from the ribosomal site.

scholarly journals Large facilities and the evolving ribosome, the cellular machine for genetic-code translation

2009 ◽  
Vol 6 (suppl_5) ◽  
Author(s):  
Ada Yonath
Keyword(s):  
Synchrotron Radiation ◽  
Genetic Code ◽  
Structural Information ◽  
Peptide Bond ◽  
Polymerase Activity ◽  
Resistance Mechanisms ◽  
Peptide Bond Formation ◽  
Peptide Bonds ◽  
Polypeptide Chains

Well-focused X-ray beams, generated by advanced synchrotron radiation facilities, yielded high-resolution diffraction data from crystals of ribosomes, the cellular nano-machines that translate the genetic code into proteins. These structures revealed the decoding mechanism, localized the mRNA path and the positions of the tRNA molecules in the ribosome and illuminated the interactions of the ribosome with initiation, release and recycling factors. They also showed that the ribosome is a ribozyme whose active site is situated within a universal symmetrical region that is embedded in the otherwise asymmetric ribosome structure. As this highly conserved region provides the machinery required for peptide bond formation and for ribosome polymerase activity, it may be the remnant of the proto-ribosome, a dimeric pre-biotic machine that formed peptide bonds and non-coded polypeptide chains. Synchrotron radiation also enabled the determination of structures of complexes of ribosomes with antibiotics targeting them, which revealed the principles allowing for their clinical use, revealed resistance mechanisms and showed the bases for discriminating pathogens from hosts, hence providing valuable structural information for antibiotics improvement.

Address of the President Lord Todd at the Anniversary Meeting, 30 November 1976

1977 ◽  
Vol 196 (1122) ◽  
pp. 1-12
Keyword(s):  
Protein Interactions ◽  
Complex Analysis ◽  
Organic Molecules ◽  
Heavy Atom ◽  
Vitamin B ◽  
Protein Protein Interactions ◽  
X Ray Crystallography ◽  
Polypeptide Chains ◽  
Complex Organic

The Copley Medal is awarded to Professor Dorothy M. C. Hodgkin, O. M., F. R. S. Professor Dorothy Hodgkin is distinguished for her research on the structure of complex organic molecules by the method of X-ray crystallography. She was among the first to appreciate the importance of heavy-atom phase-determining methods and these she used to effect the first complete determination of the stereochemistry of a sterol derivative in her analysis of cholesteryl iodide. The same powerful method of analysis and in particular her extraordinary gift of being able to interpret correctly the complex, partially resolved and often misleading electron density patterns that are first obtained, have been responsible for her success in elucidating the structures of many other important natural products, especially penicillin and vitamin B 12 . This last is by far the most beautiful and complex analysis which has yet been completed in this field and it is of fundamental importance to chemical science. In recent years Professor Hodgkin’s main interest has been devoted to the structure of insulin, on which she has been working on and off since 1935. Carried out with characteristic precision, this work has become a mine of stereochemical information relating to contacts between polypeptide chains and is of great significance for our interpretation of protein-protein interactions.

Determination of Antibody Specificity by Western Blotting

Cell Biology ◽  
2006 ◽  
pp. 527-532 ◽  
Author(s):  
J CELIS ◽  
J MOREIRA ◽  
P GROMOV
Keyword(s):  
Western Blotting ◽  
Antibody Specificity

scholarly journals Amino Acid Sequence of a Feather Keratin From Silver Gull (Larus novae-hollandiae) and Comparison with One from Emu (Dromaius novae-hollandiae)

1974 ◽  
Vol 27 (4) ◽  
pp. 369 ◽  
Author(s):  
IJ O'Donnell ◽  
AS Inglis
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Tryptic Digestion ◽  
Crystalline Region ◽  
Feather Keratin ◽  
Matrix Region ◽  
Polypeptide Chains ◽  
Selection Of

The amino acid sequence of the major components of the silver gull feather calamus has been determined and compared with that of the emu. The sequenator was used with a modified Edman-Begg program to facilitate determination of the sequence of the large hydrophobic fragment obtained on tryptic digestion. The main features of the comparison were: (1) the overall structures of the polypeptide chains were similar, having non-crystalline cystine-rich sections towards either end of the chain separated by a large crystalline region of 62 residues which contained the majority of the hydrophobic and serine and glycine residues; (2) approximately one-sixth of the residues were different in the two species, with the majority of changes occurring in the tails (i.e. non-crystalline or matrix region). The data argue for stringent demands in the selection of amino acids for the crystalline part of the feather molecule, a severity that is probably comparable to the strict requirements for the sequence of some of the enzymes.

scholarly journals Molecular weight determination of polypeptide chains of molluscan and arthropod hemocyanins

FEBS Letters ◽  
1972 ◽  
Vol 22 (1) ◽  
pp. 5-7 ◽  
Author(s):  
B. Salvato ◽  
S. Sartore ◽  
M. Rizzotti ◽  
Anna Ghiretti Magaldi
Keyword(s):  
Molecular Weight ◽  
Molecular Weight Determination ◽  
Polypeptide Chains

scholarly journals Haemoglobin from the tadpole shrimp, Lepidurus apus lubbocki Characterization of the molecule and determination of the number of polypeptide chains

1979 ◽  
Vol 183 (2) ◽  
pp. 325-330 ◽  
Author(s):  
E Ilan ◽  
E Daniel
Keyword(s):  
Molecular Weight ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Sedimentation Coefficient ◽  
Sedimentation Equilibrium ◽  
Guanidinium Chloride ◽  
Tadpole Shrimp ◽  
Polypeptide Chains

Haemoglobin from the tadpole shrimp, Lepidurus apus lubbocki, was found to have a sedimentation coefficient (s020,w) of 19.3 +/- 0.2 S and a molecular weight, as determined by sedimentation equilibrium, of 798000 +/- 20000. The amino acid composition showed the lack of cysteine and cystine residues. A haem content of 3.55 +/- 0.03% was determined, corresponding to a minimal mol.wt. of 17400 +/- 200. The pH-independence in the range pH 5-11 of the sedimentation coefficient indicates a relatively high stability of the native molecule. Sodium dodecyl sulphate/polyacrylamide-gel electrophoresis gave one band with mobility corresponding to a mol.wt. of 34000 +/- 1500. The molecular weight of the polypeptide chain was determined to be 32800 +/- 800 by sedimentation equilibrium in 6 M-guanidinium chloride and 0.1 M-2-mercaptoethanol. The findings indicate that Lepidurus haemoglobin is composed of 24 identical polypeptide chains, carrying two haem groups each.

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