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- 저자 : Adriana K. Carmona (검색결과 2 건)
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Maria Fernanda de M. Costa,Adriana K. Carmona,Marcio F. M. Alves,Timothy M. Ryan,Helen M. Davies,Garry A. Anderson,Ron F. Slocombe 대한수의학회 2011 Journal of Veterinary Science Vol.12 No.1
Angiotensin-I converting enzyme (ACE) is a key regulator of blood pressure, electrolytes and fluid homeostasis through conversion of angiotensin I into angiotensin II. Recently, a genetic polymorphism of the ACE gene, which accounts for 47% of the variation of ACE activity in blood, has been advocated as a biomarker of athletic aptitude. Different methods of analysis and determination of ACE activity in plasma have been used in human and equine research without a consensus of a “gold standard” method. Different methods have often been used interchangeably or cited as being comparable in the existing literature; however, the actual agreement between assays has not been investigated. Therefore, in this study, we evaluated the level of agreement between three different assays using equine plasma obtained from 29 horses. Two spectrophotometric assays using Furylacryloylphenylalanyl-glycyl-glycine as substrate and one fluorimetric assay utilizing o-aminobenzoic acid-FRK-(Dnp)P-OH were employed. The results revealed that the measurements from the different assays were not in agreement, indicating that the methods should not be used interchangeably for measurement of equine ACE activity. Rather, a single method of analysis should be adopted to achieve comparable results and critical appraisal of the literature is needed when attempting to compare results obtained from different assays.
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Bersanetti, Patrí,cia A.,Park, Ho-Yong,Bae, Kyung Sook,Son, Kwang-Hee,Shin, Dong-Ha,Hirata, Izaura Y.,Juliano, Maria A.,Carmona, Adriana K.,Juliano, Luiz Elsevier 2005 Enzyme and microbial technology Vol.37 No.6
<P><B>Abstract</B></P><P>We investigated the biochemical properties of a 51.5kDa metalloprotease (arazyme, 3.4.24.40) secreted into the culture medium by <I>Aranicola proteolyticus</I>, a symbiotic bacterium of the spider <I>Nephila clavata</I>. The enzyme was purified to apparent homogeneity by ion exchange chromatography in a Resource Q column (FPLC system). The substrate specificity requirements of purified arazyme were examined using fluorescence resonance energy transfer (FRET) peptides derived from the lead sequence Abz-KLRFSKQ-EDDnp (Abz=<I>ortho</I>-aminobenzoic acid; EDDnp=ethylenediaminedinitrophenyl). Three series of peptides were assayed to map the S<SUB>2</SUB>, S<SUB>1</SUB> and <SUB><SUP>S′</SUP>1</SUB> subsites: Abz-KXRFSKQ-EDDnp, Abz-KLXFSKQ-EDDnp and Abz-KLRXSKQ-EDDnp (X are natural amino acids). The results indicated that S<SUB>1</SUB> subsite has a broad specificity, being Gly the preferred amino acid for this subsite followed by positively charged residues (Arg and His). The S<SUB>2</SUB> and <SUB><SUP>S′</SUP>1</SUB> subsites accommodated better hydrophobic residues with aliphatic or aromatic side chains (Leu, Phe). The pH effect on hydrolysis of Abz-KLFFSKQ-EDDnp indicated that optimal hydrolysis occurred at pH 8.0 or higher. The effect of NaCl on the arazyme activity depends on the substrate, but in general the activity was reduced with this salt. The temperature did not affect the enzyme from 10 to 45°C, after which activity decreased sharply. Arazyme presented high hydrolytic activity on substance P and peptides related to bradykinin. In addition, arazyme activity was resistant to the treatment by pepsin, trypsin and chymotrypsin. In conclusion, arazyme has a broad hydrolytic profile and works in very aggressive conditions, which justify its potential use in therapeutics and biotechnological applications.</P>
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