[3H]Ryanodine Binding Sites of SR Vesicles of the Chicken Pectoral Muscle

• 영문명: [³H]Ryanodine Binding Sites of SR Vesicles of the Chicken Pectoral Muscle
• 발행기관: 대한생리학회-대한약리학회
• 저자명: Hyo-Yung Yun Jong-Rye Jeon Jang-Hee Hong Gang-Min Hur Jae-Heun Lee Jeong-Ho Seok
• 간행물 정보: 『The Korean Journal of Physiology & Pharmacology』제1권 제4호, 377~384쪽, 전체 8쪽
• 주제분류: 의약학 > 의학일반
• 파일형태: PDF
• 발행일자: 1997.01.01

영문 초록

To investigate the properties of ryanodine binding sites of the bird skeletal SR vesicles, SDS PAGE, purification of RyR, and [³H]ryanodine binding study were carried out in the SR vesicles prepared from the chicken pectoral muscle. The chicken SR vesicles have two high molecular weight (HMW) protein bands as in eel SR vesicles on SDS PAGE. The HMW bands on SDS PAGE were found in the [³H] ryanodine peak fraction (Fr_3-5) obtained from the purification step of the ryanodine receptor protein. Bmax and K_D of the chicken [³H]ryanodine binding sites were 12.52 pmol/mg protein and 14.53 nM, respectively. Specific [³H]ryanodine binding was almost maximal at 50∼100 ՌM Ca²⁺, but was not increased by 5 mM AMP and not inhibited by high Ca²⁺. Binding was significantly inhibited by 20∼100 ՌM ruthenium red and 1 mM tetracaine, but slightly inhibited by Mg²⁺. From the above results, it is suggested that chicken SR vesicles have the ryanodine binding sites to which the binding of ryanodine is almost maximal at 50∼10 ՌM Ca²⁺, is significantly inhibited by ruthenium red and tetracaine, slightly inhibited by Mg²⁺, but not affected by AMP and not inhibited by high Ca²⁺.

키워드

Ca-release channel Ryanodine receptor Sarcoplasmic reticulum Chicken Abbreviation AMP Adenosine-5 -monophosphate DIFP Diisopropyl fluorophosphate EGTA Ethylene glycol-bis(Ղ -aminoethyl ether) N,N,N ,N -tetraacetic acid PMSF Phenylmethys