1.Brain abscess complicating intracerebral hemorrhage.
Ae Young LEE ; Jong Heun JEON ; Jae Moon KIM
Journal of the Korean Neurological Association 1997;15(2):417-420
Brain abscess is a common bacterial infection of the central nervous system. Previously, the most common source of brain abscess is from the otorrhinologic infection, the hematogenous spread of infection from a distant site to the central ner vous system is increased(Alvord & Shaw, 1977; Zimmerman & Weingerten, 1991). Since intact brain parenchyma is usually resistant to inecton, focal areas of ischemia or necrosis are a prequisite to invasion by pathogenic microorganisms(Patric & Kaplan, 1988). There have been a few reports about the stroke lesions changed into brain abscess(Chen et al, 1995; Scully et al. 1991). We report serial brain images with the clinical observations in a patient with a transformation of spontaneous intracerebral hemorrhage into brain abscess.
Bacterial Infections
;
Brain Abscess*
;
Brain*
;
Central Nervous System
;
Cerebral Hemorrhage*
;
Humans
;
Ischemia
;
Necrosis
;
Stroke
2.(3H)Ryanodine binding sites of SR vesicles of the chicken pectoral muscle.
Hyo Yung YUN ; Jong Rye JEON ; Jang Hee HONG ; Gang Min HUR ; Jae Heun LEE ; Jeong Ho SEOK
The Korean Journal of Physiology and Pharmacology 1997;1(4):377-384
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 (Fr3-5) obtained from the purification step of the ryanodine receptor protein. Bmax and KD 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 micrometer Ca2+, but was not increased by 5 mM AMP and not inhibited by high Ca2+. Binding was significantly inhibited by 20~100 micrometer 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 micrometer Ca2+, is significantly inhibited by ruthenium red and tetracaine, slightly inhibited by Mg2+, but not affected by AMP and not inhibited by high Ca2+.
Binding Sites*
;
Birds
;
Chickens*
;
Eels
;
Electrophoresis, Polyacrylamide Gel
;
Molecular Weight
;
Ruthenium Red
;
Ryanodine
;
Ryanodine Receptor Calcium Release Channel
;
Sarcoplasmic Reticulum
;
Tetracaine