Complete cDNA sequence of bovine α1-antitrypsin

Sinha, Dipali; Bakhshi, Meenakshi R.; Kirby, Edward P.

doi:10.1016/0167-4781(92)90530-d

Cited by 15 publications

(12 citation statements)

References 9 publications

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“…Bovine α 1 -PI [e] AIPM SLPPDVEFNRPFLCILYDRNTKSPLFVGKVVNPT a Mak et al 2004 b Huang et al 1995b c Bollen et al 1983;Carrell et al 1982d Brown et al 1989 e Sinha et al 1992 Proteinase inhibitors of the serpin group interact with proteinases as suicide substrates with a very high affinity, and proteinase usually cleaves at least one peptide bond in the inhibitor protein-the bait amino acid bond between P1 and P1 0 residues in the reactive loop. Stable covalent enzyme-inhibitor complexes are formed during that reaction and these complexes do not disintegrate even in the presence of SDS and high temperature.…”

Section: Aipm Slppdvefnrpflcilydrntksplfvgkvvnptmentioning

confidence: 99%

Purification and characterization of α1-proteinase inhibitor and antithrombin III: major serpins of rainbow trout (Oncorhynchuss mykiss) and carp (Cyprinus carpio) blood plasma

Mickowska

2008

Fish Physiol Biochem

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The main serine proteinase inhibitors of rainbow trout (Oncorhynchuss mykiss) and common carp (Cyprinus carpio) blood plasma were isolated and purified. The investigated inhibitors, alpha(1)-proteinase inhibitor (alpha(1)-PI) and antithrombin III (AT III), act by forming stable complexes with target proteinases. The association rate constants k (on) for the interaction of fish plasma inhibitors with several serine proteinases have been determined: k (on) for both carp and rainbow trout alpha(1)-PI were >10(7) M(-1) s(-1) for human neutrophil elastase, and in the case of bovine trypsin and chymotrypsin k (on) values were 2.0-5.2 x 10(6) M(-1) s(-1). Association rate constants k (on) for the interaction of carp and rainbow trout AT III with bovine trypsin and thrombin were about 1.3 x 10(4)-7.9 x 10(5) M(-1) s(-1) without and >10(7) M(-1) s(-1) in presence of heparin; so antithrombins require the presence of heparin to become effective proteinase inhibitors. The high degree of homology of the estimated amino acid sequences of fish inhibitors reactive site loops confirms their similarity with other proteinase inhibitors from the serpin family.

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Section: Aipm Slppdvefnrpflcilydrntksplfvgkvvnptmentioning

confidence: 99%

Purification and characterization of α1-proteinase inhibitor and antithrombin III: major serpins of rainbow trout (Oncorhynchuss mykiss) and carp (Cyprinus carpio) blood plasma

Mickowska

2008

Fish Physiol Biochem

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“…When there was no available restriction enzyme site for PCR-RFLP analysis, CRS combined with PCR amplification is a simple and efficient method that could be used to detect single nucleotide polymorphisms (SNPs) genotypes [8]. One-mismatch bases are used in a primer P3 in this study to create a restriction site for PCR.…”

Section: Methodsmentioning

confidence: 99%

“…Sinha et al [8] had isolated a whole cDNA clone coding for bovine α1-AT from a λgt11 bovine liver cDNA library using a human α1-AT cDNA as a probe. Five single nucleotide polymorphisms (SNPs) in coding regions of the bovine α1 - AT gene were found by direct sequencing of reverse transcription-polymerase chain reaction (RT-PCR) products from a wide range of cattle tissues.…”

Section: Introductionmentioning

confidence: 99%

Two single nucleotide polymorphisms sites in α1-AT gene and their association with somatic cell score in Chinese Holstein cows

Guo

Lang

et al. 2017

J of Biol Res-Thessaloniki

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BackgroundAlpha 1-antitrypsin (α1-AT) may affect the susceptibility of mastitis in dairy cattle for its possible role in the protection of lactoferrin from proteolytic degradation in the mammary. Milk somatic cell score (SCS) is a logarithmic transformation of the milk somatic cell count widely used as an index to evaluate mastitis. To study the relationships of α1-AT gene and SCS in Chinese Holstein cows, methods of PCR-SSCP, DNA sequencing, PCR-RFLP, and CRS-PCR technologies were used to detect single nucleotide polymorphisms sites in α1-AT gene.ResultsTwo polymorphic sites at G5503A and G5746C of α1-AT gene were found. AA (0.3633), AB (0.4644) and BB (0.1723) genotypes were detected at G5503A site, CC (0.3483), CD (0.4906) and DD (0.1611) genotypes were found at G5746C in Chinese Holstein cows. Least squares mean of SCS for individuals with BB genotype was significantly lower than that with AA and AB genotype (p < 0.01), and that with AB genotype was significantly lower than that with AA (p < 0.05). There was no significant difference among individuals with CC, CD and DD genotypes (p > 0.05). Least squares mean of SCS for individuals with BBDD genotype combination were significantly lower than those with AACC and AACD (p < 0.05).ConclusionsStatistical analysis indicated that B allele and BBDD genotype combination of α1-AT can improve mastitis resistance in dairy cattle.

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“…This issue is comThe serpins are a family of proteins that are widely plex, even at the level of gene copy number. For examdistributed throughout the plant and animal king-ple, there is a single functional a1AT gene in rats (Chao doms, and they perform a diverse array of functions in et al, 1990), cows (Sinha et al, 1992), sheep (Brown et vivo (Potempa et al, 1994). In spite of these functional al., 1989), and primates, including baboons (Kurachi et and evolutionary differences, the various serpin pro-al., 1981) and humans (assuming that ATR is a pseuteins are highly conserved in both primary sequence dogene, Bao et al, 1988).…”

Section: Figmentioning

confidence: 98%

A 370-kb Cosmid Contig of the Serpin Gene Cluster on Human Chromosome 14q32.1: Molecular Linkage of the Genes Encoding α1-Antichymotrypsin, Protein C Inhibitor, Kallistatin, α1-Antitrypsin, and Corticosteroid-Binding Globulin

Rollini

Fournier

1997

Genomics

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Complete cDNA sequence of bovine α1-antitrypsin

Cited by 15 publications

References 9 publications

Purification and characterization of α1-proteinase inhibitor and antithrombin III: major serpins of rainbow trout (Oncorhynchuss mykiss) and carp (Cyprinus carpio) blood plasma

Purification and characterization of α1-proteinase inhibitor and antithrombin III: major serpins of rainbow trout (Oncorhynchuss mykiss) and carp (Cyprinus carpio) blood plasma

Two single nucleotide polymorphisms sites in α1-AT gene and their association with somatic cell score in Chinese Holstein cows

A 370-kb Cosmid Contig of the Serpin Gene Cluster on Human Chromosome 14q32.1: Molecular Linkage of the Genes Encoding α1-Antichymotrypsin, Protein C Inhibitor, Kallistatin, α1-Antitrypsin, and Corticosteroid-Binding Globulin

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