Purification of acethylcholinesterase from the mollusc  Mytilus galloprovincialis Lam. and investigation of its  kinetic properties

Sezin Anıl; Nurten Ozsoy

Makale detayları

Purification of acethylcholinesterase from the mollusc Mytilus galloprovincialis Lam. and investigation of its kinetic properties

Yazarlar:

Sezin Anıl | Nurten Ozsoy

Yayıncı:

Marmara University

Ana Başlıklar:

Pharmaceutical Biochemistry | Pharmacognosy

Dergi:

Journal of Research in Pharmacy Vol.23 Issue 4, pp.759-769

Belge Tipi:

Makale

Yayın Tarihi:

6/2025

Belge Dili:

İngilizce

Document ID (Org No.):

2001347694

pISSN:

2630-6344

Anahtar kelimeler:

Özet:

 The role of acetylcholinesterase in terminating acetylcholine-mediated neurotransmission made it the focus of intense research. In this study the haemolymph Acetylcholinesterase AChE from the mollusc Mytilus galloprovincialis was purified to homogeneity by NH42SO4 fractional precipitation and affinity chromatography on edrophonium-Sepharose 6B. The enzyme was purified approximatedly 13 fold over the crude extract and was obtained in 3  yield. The specific activity of purified enzyme was 3 Umg protein. It had an optimum pH of 7.5 and showed optimal activity at 35oC. Km and Vmax for acetylthiocholine iodide were 1.3 mM and 0.188 mMmgmin, respectively. The purified enzyme migrated as a 51 000 dalton band during polyacrylamide gel electrophoresis under denaturing and reducing conditions. Three methoxyflavones were examined in order to evaluate their potential as anti-Alzheimers Disease AD agents. All of the compounds were shown to be potent AChE inhibitors. Therefore, these compounds may have great value in the development of therapeutic and preventive agents for AD.

 The role of acetylcholinesterase in terminating acetylcholine-mediated neurotransmission made it the focus of intense research. In this study the haemolymph Acetylcholinesterase AChE from the mollusc Mytilus galloprovincialis was purified to homogeneity by NH42SO4 fractional precipitation and affinity chromatography on edrophonium-Sepharose 6B. The enzyme was purified approximatedly 13 fold over the crude extract and was obtained in 3  yield. The specific activity of purified enzyme was 3 Umg protein. It had an optimum pH of 7.5 and showed optimal activity at 35oC. Km and Vmax for acetylthiocholine iodide were 1.3 mM and 0.188 mMmgmin, respectively. The purified enzyme migrated as a 51 000 dalton band during polyacrylamide gel electrophoresis under denaturing and reducing conditions. Three methoxyflavones were examined in order to evaluate their potential as anti-Alzheimers Disease AD agents. All of the compounds were shown to be potent AChE inhibitors. Therefore, these compounds may have great value in the development of therapeutic and preventive agents for AD.

 The role of acetylcholinesterase in terminating acetylcholine-mediated neurotransmission made it the focus of intense research. In this study the haemolymph Acetylcholinesterase AChE from the mollusc Mytilus galloprovincialis was purified to homogeneity by NH42SO4 fractional precipitation and affinity chromatography on edrophonium-Sepharose 6B. The enzyme was purified approximatedly 13 fold over the crude extract and was obtained in 3  yield. The specific activity of purified enzyme was 3 Umg protein. It had an optimum pH of 7.5 and showed optimal activity at 35oC. Km and Vmax for acetylthiocholine iodide were 1.3 mM and 0.188 mMmgmin, respectively. The purified enzyme migrated as a 51 000 dalton band during polyacrylamide gel electrophoresis under denaturing and reducing conditions. Three methoxyflavones were examined in order to evaluate their potential as anti-Alzheimers Disease AD agents. All of the compounds were shown to be potent AChE inhibitors. Therefore, these compounds may have great value in the development of therapeutic and preventive agents for AD.

 The role of acetylcholinesterase in terminating acetylcholine-mediated neurotransmission made it the focus of intense research. In this study the haemolymph Acetylcholinesterase AChE from the mollusc Mytilus galloprovincialis was purified to homogeneity by NH42SO4 fractional precipitation and affinity chromatography on edrophonium-Sepharose 6B. The enzyme was purified approximatedly 13 fold over the crude extract and was obtained in 3  yield. The specific activity of purified enzyme was 3 Umg protein. It had an optimum pH of 7.5 and showed optimal activity at 35oC. Km and Vmax for acetylthiocholine iodide were 1.3 mM and 0.188 mMmgmin, respectively. The purified enzyme migrated as a 51 000 dalton band during polyacrylamide gel electrophoresis under denaturing and reducing conditions. Three methoxyflavones were examined in order to evaluate their potential as anti-Alzheimers Disease AD agents. All of the compounds were shown to be potent AChE inhibitors. Therefore, these compounds may have great value in the development of therapeutic and preventive agents for AD.

Makale detayları

Purification of acethylcholinesterase from the mollusc Mytilus galloprovincialis Lam. and investigation of its kinetic properties

Yazarlar:

Sezin Anıl | Nurten Ozsoy

Yayıncı:

Marmara University

Ana Başlıklar:

Pharmaceutical Biochemistry | Pharmacognosy

Dergi:

Journal of Research in Pharmacy Vol.23 Issue 4, pp.759-769

Belge Tipi:

Makale

Yayın Tarihi:

6/2025

Belge Dili:

İngilizce

Document ID (Org No.):

2001347694

pISSN:

2630-6344

Acethylcholinesterase

Mytilus galloprovincialis Lam.

enzyme purification

kinetic properties

inhibition by methoxyflavones.

Sayı

Makale detayları

Purification of acethylcholinesterase from the mollusc Mytilus galloprovincialis Lam. and investigation of its kinetic properties

Yazarlar: Sezin Anıl | Nurten Ozsoy

Yayıncı: Marmara University

Ana Başlıklar: Pharmaceutical Biochemistry | Pharmacognosy

Dergi: Journal of Research in Pharmacy Vol.23 Issue 4, pp.759-769

Belge Tipi: Makale

Yayın Tarihi: 6/2025

Belge Dili: İngilizce

Document ID (Org No.): 2001347694

pISSN: 2630-6344

Acethylcholinesterase

Mytilus galloprovincialis Lam.

enzyme purification

kinetic properties

inhibition by methoxyflavones.

Sayı

Yazarlar:

Sezin Anıl | Nurten Ozsoy

Yayıncı:

Marmara University

Ana Başlıklar:

Pharmaceutical Biochemistry | Pharmacognosy

Dergi:

Journal of Research in Pharmacy Vol.23 Issue 4, pp.759-769

Belge Tipi:

Makale

Yayın Tarihi:

6/2025

Belge Dili:

İngilizce

Document ID (Org No.):

2001347694

pISSN:

2630-6344