Charcterization of kinetic parameters of sleep liver kidnem and lung acetyl coenzyme a dependent (:) arylamine n-acetyltransferases
Koyun karaciğer, böbrek ve akciğer asetil coenzim A (:) arilamin n-asetiltransferaz enzimlerinin kinetik parametrelerinin karakterize edilmesi
- Tez No: 56803
- Danışmanlar: DOÇ. DR. TÜLİN GÜRAY
- Tez Türü: Yüksek Lisans
- Konular: Biyoloji, Biology
- Anahtar Kelimeler: Belirtilmemiş.
- Yıl: 1996
- Dil: İngilizce
- Üniversite: Orta Doğu Teknik Üniversitesi
- Enstitü: Fen Bilimleri Enstitüsü
- Ana Bilim Dalı: Biyoloji Ana Bilim Dalı
- Bilim Dalı: Belirtilmemiş.
- Sayfa Sayısı: 95
Özet
enzyme activity in these different tissue types. The effect of p- aminobenzoic acid (PABA) and acetyl coenzyme A concentrations, pH, temperature, amount of enzyme and reaction period on the enzyme activity were also studied and the optimum conditions for maximum activity of isolated sheep liver, kidney and lung NATs were determined. The spectrophotometric assay procedure was used for the enzyme activity measurements and specific activities of liver, kidney and lung NATs were found as 5.3xl0~3 nmoles/min/mg protein, 3.4xl0“3 nmoles/min/mg protein, 2.5xl0”3 nmoles/min/mg protein, respectively. The NAT activities were determined using p-aminobenzoic acid (PABA) as a general substrate. The rate of N-acetylation reaction was linear up to approximately 70 jig of liver, 80 jig of kidney and 88 ug lung cytosolic protein. Also, sulfamethazine (SMZ) was used as a substrate in order to study the polymorphic pattern of the NAT activities in different tissues. Sheep kidney and lung NATs by PABA and sheep liver NATS by both PABA and SMZ seemed to be saturated at 0.1 mM concentration. The kinetic constants for liver, kidney and lung NATs were determined by using p-aminobenzoic acid (PABA) as a substrate. V max values were found as 5.2xl0“3, 3.4xl0”3 and 2.5xl0“3 nmoles/min/mg and K m values were found as 53, 34, 28 uM for liver, kidney and lung, respectively. IVEnzim aktivitesinin en yüksek olduğu optimum koşullar, farklı p- amino-benzoik asit (PABA) ve asetil coenzim A konsantrasyonları, pH değerleri, değişik ısı değerleri, enzim miktarları ve reaksiyon zamanlan kullanılarak belirlenmiştir. NAT aktivitelerinin saptanması için spektrofotometrik deney metodu kullanılmış ve özgün NAT aktivitesinin karaciğerde 5.3x1 0”3 nmol/dak/mg protein, böbrekte 3.4xl0“3 nmol/dak/mg protein ve akciğerde 2.5xl0~3 nmol/dak/mg protein olduğu bulunmuştur. Enzim aktivitesi asetil coenzim A (:) arilamin N-asetiltransferazın genel substratı olan p-aminobenzoik asit (PABA) kullanılarak tayin edilmiştir. Reaksiyon hızının karaciğerde 70 ug, böbrekte 80 ug ve akciğerde 88 ug sitozol proteinine kadar doğru orantılı arttığı görülmüştür. NAT aktivitelerinin farklı doku çeşitlerinde, polymorfik dağılımını belirlemek için sulfamethazine (SMZ) substrat olarak kullanılmıştır. Koyun böbrek ve akciğer NAT larının 0.1 mM PABA ve koyun karaciğer NAT ınında 0.1 mM PABA ve 0.1 mM SMZ konsantrasyonlarında doygunluğa ulaştıkları gözlenmiştir. Karaciğer, böbrek ve akciğer NAT lannda PABA için Vmax ve Km değerleri, sırasıyla 5.2xl0”3 nmol/dak/mg protein ve 53 uM, 3.4xl0“3 nmol/dak/mg protein ve 34 uM, 2.5xl0-3 nmol/dak/mg protein ve 28 uM olarak hesaplanmıştır. Bu üç farklı koyun doku çeşidi için 6.0 ve 9.5 pH değerleri arasında aktivite-pH etkinlik eğrileri saptanmış ve en yüksek enzim aktiviteleri pH 7. 5 'da elde edilmiştir. viienzyme activity in these different tissue types. The effect of p- aminobenzoic acid (PABA) and acetyl coenzyme A concentrations, pH, temperature, amount of enzyme and reaction period on the enzyme activity were also studied and the optimum conditions for maximum activity of isolated sheep liver, kidney and lung NATs were determined. The spectrophotometric assay procedure was used for the enzyme activity measurements and specific activities of liver, kidney and lung NATs were found as 5.3xl0~3 nmoles/min/mg protein, 3.4xl0”3 nmoles/min/mg protein, 2.5xl0“3 nmoles/min/mg protein, respectively. The NAT activities were determined using p-aminobenzoic acid (PABA) as a general substrate. The rate of N-acetylation reaction was linear up to approximately 70 jig of liver, 80 jig of kidney and 88 ug lung cytosolic protein. Also, sulfamethazine (SMZ) was used as a substrate in order to study the polymorphic pattern of the NAT activities in different tissues. Sheep kidney and lung NATs by PABA and sheep liver NATS by both PABA and SMZ seemed to be saturated at 0.1 mM concentration. The kinetic constants for liver, kidney and lung NATs were determined by using p-aminobenzoic acid (PABA) as a substrate. V max values were found as 5.2xl0”3, 3.4xl0“3 and 2.5xl0”3 nmoles/min/mg and K m values were found as 53, 34, 28 uM for liver, kidney and lung, respectively. IV
Özet (Çeviri)
ABSTRACT CHARACTERIZATION OF KINETIC PARAMETERS OF SHEEP LIVER, KIDNEY AND LUNG CYTOSOLIC ACETYL COENZYME A DEPENDENT (:) ARYLAMINE N-ACETYLTRANSFERASES Güvenç, Tuğba M. S., Department of Biology Supervisor : Assoc. Prof. Dr. Tülin Güray January 1996, 80 pages Biological acetylation is one of the major conjugation reactions of animal species including humans. Acetyl coenzyme A dependent (:) arylamine N-acetyltransferase (NAT) (E.C.2.3.1.5.) is the enzyme which catalyzes the acetyl coenzyme A dependent arylamine N-acetyl transfer in acetylation reactions. In this study, acetyl coenzyme A dependent (:) atylamine N-acetyl- transferases were isolated from sheep liver, kidney and lung in order to study some of the biochemical properties of this enzyme and compare the iiienzyme activity in these different tissue types. The effect of p- aminobenzoic acid (PABA) and acetyl coenzyme A concentrations, pH, temperature, amount of enzyme and reaction period on the enzyme activity were also studied and the optimum conditions for maximum activity of isolated sheep liver, kidney and lung NATs were determined. The spectrophotometric assay procedure was used for the enzyme activity measurements and specific activities of liver, kidney and lung NATs were found as 5.3xl0~3 nmoles/min/mg protein, 3.4xl0“3 nmoles/min/mg protein, 2.5xl0”3 nmoles/min/mg protein, respectively. The NAT activities were determined using p-aminobenzoic acid (PABA) as a general substrate. The rate of N-acetylation reaction was linear up to approximately 70 jig of liver, 80 jig of kidney and 88 ug lung cytosolic protein. Also, sulfamethazine (SMZ) was used as a substrate in order to study the polymorphic pattern of the NAT activities in different tissues. Sheep kidney and lung NATs by PABA and sheep liver NATS by both PABA and SMZ seemed to be saturated at 0.1 mM concentration. The kinetic constants for liver, kidney and lung NATs were determined by using p-aminobenzoic acid (PABA) as a substrate. V max values were found as 5.2xl0“3, 3.4xl0”3 and 2.5xl0"3 nmoles/min/mg and K m values were found as 53, 34, 28 uM for liver, kidney and lung, respectively. IV
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