ABSTRACT
Serum specimens from 752 individuals undergoing coronary arteriography were examined for antibodies to Chlamydia pneumoniae. Patients with coronary artery disease (CAD) were more likely to have IgG antibodies to C. pneumoniae than were individuals without CAD (60% vs. 52%; P=.007; odds ratio, 1.8; 95% confidence interval, 1. 17-2.77). Antibodies to recombinant hsp60 of C. pneumoniae were found with nearly the same frequency in patients with CAD and individuals without CAD (29% vs. 30%; P=.751). There was no association between chlamydial hsp60 antibodies and the severity of CAD or a previous myocardial infarction. Patient sera reacted most frequently to C. pneumoniae proteins of 17, 38, 40, 58, and 60/62 kDa. Reactivity to these proteins was not different between patients with and without CAD. Study results indicate that neither antibodies to chlamydial hsp60 nor antibodies to other C. pneumoniae proteins are useful for discriminating between seropositive patients with and without CAD.
Subject(s)
Antibodies, Bacterial/blood , Chaperonin 60/immunology , Chlamydophila pneumoniae/immunology , Coronary Disease/immunology , Immunoglobulin G/blood , Antibody Formation , Coronary Angiography , Coronary Disease/blood , Female , Humans , Immunoenzyme Techniques , Male , Middle Aged , Recombinant Proteins/immunology , Reference ValuesABSTRACT
The primary structure of the haemoglobin of the African Elephant (Loxodonta africana) is reported. The sequence was determined by means of a sequenator. The haemoglobin differs in 26 amino acids in the alpha-chains and in 27 in the beta-chains from that of adult human haemoglobin. The haemoglobin of the African Elephant, like that of the Indian Elephant and Ilama, has only 5 binding sites for polyphosphate. This finding explains the low p(O2)50 value in whole blood as a result of the lower 2,3-bisphosphoglycerate-haemoglobin interaction. This is discussed in relation to aspects of respiratory physiology; some points are also of interest with regard to the Second Punic War and Hannibal's crossing of the Alps.
Subject(s)
Asparagine , Diphosphoglyceric Acids/blood , Elephants/blood , Hemoglobins , 2,3-Diphosphoglycerate , Altitude , Amino Acid Sequence , Amino Acids/analysis , Animals , Drug Interactions , Hemoglobins/metabolism , Hydrolysis , Oxygen/blood , Protein Binding , Protein Conformation , TrypsinABSTRACT
The primary structure of the hemoglobin of the Indian Elephant (Elephas maximus) is given. The sequence was determined automatically in a sequenator. By homologous comparison with adult human HbA, the alpha-chains differ by 24 exchanges and the beta-chains by 27 exchanges. Furthermore, we report p(O2)50 values with regard to altered contact sites with 2,3-bisphosphoglycerate in Indian elephant hemoglobin. Our findings explain the low p(O2)50 and the reduced interaction with 2,3-bisphosphoglycerate. Elephant hemoglobin has, like that of the Llama, only five phosphate binding sites. In addition, we have made an attempt to relate these results to aspects of respiratory physiology. Some implications of these biochemical and physiological results, concerning the Second Punic War and Hannibal's Alp transition, are given.
