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De Groot, H., Van Swieten, P., & Aalberse, R. C. (1990). Evidence for a Fel d I-like molecule in the “big cats” (Felidae species). J Allergy Clin Immunol, 86(1), 107–116.
Abstract: In this study, we investigated the cross-reactivity pattern of IgE and IgG4 antibodies to the major feline allergen, Fel d I. We studied the IgE and IgG4 response of 11 cat-allergic patients against Fel d I-like structures in eight members of the Felidae family: ocelot, puma, serval, siberian tiger, lion, jaguar, snow leopard, and caracal. Hair from these “big cats” was collected, extracted, and used in a RAST system and histamine-release test. By means of a RAST-inhibition assay with affinity-purified Fel d I from cat dander, it was established that, in the Felidae species, a Fel d I equivalent is present that reacts with IgE and IgG4 antibodies. We found that all patients had cross-reacting IgE antibodies to seven of the Felidae tested; no IgE antibodies reactive with the caracal were found. Eight of 10 patients with IgG4 antibodies directed to cat dander also had IgG4 antibodies directed to several Felidae species, including the caracal. However, the correlation between the IgE and the IgG4 antibody specificity was low, indicating that, in the case of Fel d I IgE and IgG4, antibodies do not necessarily have the same specificity.
Keywords: Adolescence; Adult; Allergens; immunology; Animal; Antibodies; Monoclonal; diagnostic; use; Antibody; Specificity; Carnivora; Cats; Comparative; study; Cross; Reactions; Hair; Histamine; Release; Human; IgE; analysis; IgG; Middle; Age; Radioallergosorbent; Test; methods; Support; Non-U.S.Gov't; browse; us; government; gov't; 240
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Trepanier, L. A., Cribb, A. E., Spielberg, S. P., & Ray, K. (1998). Deficiency of cytosolic arylamine N-acetylation in the domestic cat and wild felids caused by the presence of a single NAT1-like gene. Pharmacogenetics, 8(2), 169–179.
Abstract: The purpose of this study was to determine the molecular basis for a relative deficiency in the cat of cytosolic arylamine N- acetyltransferase (NAT), an enzyme family that is important in the metabolism of xenobiotics and that normally consists of at least two related enzymes, NAT1 and NAT2. N-acetyltransferase in feline liver showed high affinity (mean Km = 2.1 microM) for p-aminobenzoic acid, an NAT1 selective substrate in humans and rabbits, but showed a very poor affinity (mean Km > 10 mM) for sulfamethazine, an NAT2 selective substrate in humans and rabbits. Immunoreactive N-acetyltransferase was detected in feline liver, bladder and colon using an NAT1-specific antipeptide antibody, but was not detected in any tissues using an NAT2- specific antibody. Southern blot analysis of genomic DNA demonstrated a single band in domestic cats using each of six restriction digests; single bands were also found on Southern blot analysis of six wild felids. The deduced amino acid sequence of the central portion of feline N-acetyltransferase, obtained by polymerase chain reaction amplification in both domestic cats and seven wild felids (lion, tiger, lynx, snow leopard, bobcat, Asian leopard cat and cheetah), contained three residues, Phe125, Arg127, and Tyr129, which determine NAT1-like substrate specificity in humans. These results support the conclusion that cytosolic arylamine N-acetylation activity is low in the cat because of the presence of a single N-acetyltransferase that has substrate specificity, immunogenicity and sequence characteristics similar to human NAT1, and that the unusual presence of only a single N- acetyltransferase gene appears to be a family wide trait shared by other felids.
Keywords: Acetylation; Amino; Acid; Sequence; Animal; Arylamine; N-Acetyltransferase; metabolism; Base; Blotting; Southern; Carnivora; genetics; Cats; Cytosol; enzymology; Dna; Human; Isoenzymes; Liver; Molecular; Data; Polymerase; Chain; Reaction; Rabbits; Homology; Nucleic Acid; Substrate; Specificity; Support; U.S.Gov't; P.H.S.; browse; nucleic; us; government; 130
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