Purification of Angiotensin-Converting Enzyme (ACE) from Sheep Kidney and Inhibition Effect of Reduced Nicotinamide Adenine Dinucleotide (NADH) on Purified ACE Activity

Kiylik A., Turkoglu V., Baş Z.

CELL BIOCHEMISTRY AND BIOPHYSICS, cilt.80, sa.1, ss.115-122, 2022 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 80 Sayı: 1
  • Basım Tarihi: 2022
  • Doi Numarası: 10.1007/s12013-021-01036-2
  • Dergi Adı: CELL BIOCHEMISTRY AND BIOPHYSICS
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, BIOSIS, Biotechnology Research Abstracts, Chemical Abstracts Core, EMBASE, MEDLINE
  • Sayfa Sayıları: ss.115-122
  • Anahtar Kelimeler: Angiotensin-converting enzyme (ACE), Reduced nicotinamide adenine dinucleotide (NADH), Antioxidant, Purification, Inhibition, OXIDATIVE STRESS, ALDOSTERONE SYSTEM, BLOOD-PRESSURE, ANTIOXIDANT, SUPPLEMENTATION, HYPERTENSION, REDUCTION, PEPTIDES, THERAPY, DISEASE
  • Van Yüzüncü Yıl Üniversitesi Adresli: Evet

Özet

Angiotensin-converting enzyme (ACE, EC 3.4.15.1) is a significant enzyme that regulates blood pressure. ACE inhibitors are often used in the treatment of hypertension. In this work, ACE was purified and characterized in one step with affinity chromatography from sheep kidneys. ACE was 10305-fold purified and specific activity was 19,075 EU/mg protein. The molecular weight and purity of ACE were found with SDS-PAGE and observed two bands at about 60 kDa and 70 kDa on the gel. The effects of reduced nicotinamide adenine dinucleotide (NADH), an antioxidant compound, on purified ACE activity were also researched. NADH on ACE activity showed an inhibition effect. The inhibition type of NADH was determined to be non-competitive inhibition by the Lineweaver-Burk chart and IC50 and K-i values for NADH were 244.33 and 175.08 mu M, respectively. These results suggest that antioxidant substances might be efficient in preventing hypertension.