STUDIES OF BRAIN LYSOSOMES—I SUBCELLULAR DISTRIBUTION OF FIVE ACID HYDROLASES, SUCCINATE DEHYDROGENASE AND GANGLIOSIDES IN RAT BRAIN *
STUDIES OF BRAIN LYSOSOMES—I SUBCELLULAR DISTRIBUTION OF FIVE ACID HYDROLASES, SUCCINATE DEHYDROGENASE AND GANGLIOSIDES IN RAT BRAIN *
复制标题
脑溶酶体的研究——I 大鼠脑内五种酸性水解酶、琥珀酸脱氢酶和神经节苷脂的亚细胞分布*
DOI:
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发表时间:
1964
影响因子:
4.7
通讯作者:
James Scott
中科院分区:
文献类型:
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作者:
H. Koenig;D. Gaines;T. Mcdonald;Rosalind Gray;James Scott
ACID phosphatase, cathepsin, and certain other acid hydrolases seem to be confined together within a special class of cytoplasmic particles, lysosomes (DE DUVE, PRESSMAN, GIANETTO, WATTIAUK and APPLEMANS, 1955). These particles have been partially separated from mitochondria and other cell constitucnts by differential centrifugation of sucrose homogenates of liver (DE DUVE et al., 1955), kidney (STRAUSS, 1954), skeletal muscle (TAPPEL, ZALKIN, CALDWELL, DESAI and SHIBKO, 1962), heart muscle (SOTTOCASA, STAGNI, ROMEO and DE BERNARD, 1962), thymus gland (RAHMAN, 1962), and several other tissues. In addition to sharing similar sedimentation properties, the particulate acid hydrolases, of which some twelve or thirteen have thus far been identified, display structural latency, i.e., they are relatively inert toward added substrates when freshly suspended in isotonic sucrose media, disruptive treatments being required to release active enzymes into solution. From the in citro behaviour of the hydrolytic enzymes, DE DUVE and associates (reviewed in DE DUVE, 1959) concluded that the lysosome is an inert osmotic sac which is delimited by an impervious lipoprotein membrane that restricts the substrate accessibility of the enclosed enzymes. Neural lysosomes have been little studied by biochemical methods. BEAUFAY, BERLEUR and DOYEN (1957) reported, in abstract form, that the hydrolases, acid phosphatase, acid RNase, acid DNase, B-glucuronidase and cathepsin, in 0.25 M sucrose homogenates of rat brain, are largely sedimentible and exhibit structural latency. However, these workers were unable to separate the acid hydrolases from mitochondria1 enzymes by differential centrifugation. WIJITTAKER (1959) subsequently found that the 0-glucuronidase and the acid phosphatase contained within a mitochondrial fraction of guinea pig brain sedimented differently i n a sucrose gradient, and so questioned the validity of the lysosome theory as applied to brain. Although the biochemical data regarding the status of the lysosome in the nervous ROSALIND GRAY and JAMES SCOTT