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Author Hochstrasser, K.; Wachter, E.; Reisinger, P.W.; Greim, M.; Albrecht, G.J.; Gebhard, W.
Title Amino acid sequences of mammalian kazal-type proteinase inhibitors from salivary glands Type Journal Article
Year 1993 Publication Comp Biochem Physiol B Abbreviated Journal
Volume 106 Issue 1 Pages 103-108
Keywords Amino; Acid; Sequence; Animal; Carnivora; Comparative; study; Cysteine; chemistry; Glycosylation; Mink; Molecular; Data; Protease; Inhibitors; Salivary; Proteins; species; Specificity; Submandibular; Gland; Trypsin; Inhibitor; Kazal; Pancreatic; browse; 200
Abstract 1. The amino acid sequences of bikazins (the double-headed Kazal-type proteinase inhibitors from submandibular glands) isolated from the snow leopard (Unica unica), the European mink (Mustela lutreola), and the European pine marten (Martes martes) were determined. 2. N-terminal domains of bikazins are characterized by a cysteine residue spacing that differs from that of C-terminal domains of bikazins and other Kazal-type proteinase inhibitor domains. 3. N-terminal sequences of bikazins seem to be specific for, and highly conserved within, each Carnivora family.
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Publisher Place of Publication Editor
Language Summary Language Original Title
Series Editor (up) Series Title Abbreviated Series Title
Series Volume Series Issue Edition
ISSN 0305-0491 ISBN Medium
Area Expedition Conference
Notes Document Type: eng Approved no
Call Number SLN @ rana @ 202 Serial 385
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Author Trepanier, L.A.; Cribb, A.E.; Spielberg, S.P.; Ray, K.
Title Deficiency of cytosolic arylamine N-acetylation in the domestic cat and wild felids caused by the presence of a single NAT1-like gene Type Journal Article
Year 1998 Publication Pharmacogenetics Abbreviated Journal
Volume 8 Issue 2 Pages 169-179
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
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.
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Publisher Place of Publication Editor
Language Summary Language Original Title
Series Editor (up) Series Title Abbreviated Series Title
Series Volume Series Issue Edition
ISSN 0960-314x ISBN Medium
Area Expedition Conference
Notes Document Type: eng Approved no
Call Number SLN @ rana @ 345 Serial 968
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