Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1979-2-12
pubmed:abstractText
To localize the membrane-bound, histone-degrading proteinase, which was previously isolated from the mitochondrial fraction, nuclei, mitochondria, lysosomes, peroxisomes, smooth and rough endoplasmic reticulum, ribosomes and plasma membranes were prepared from a rat liver homogenate according to established methods and characterized by marker enzyme activities. The isolated subcellular fractions were treated with digitonin, and subjected to a discontinuous sucrose gradient centrifugation. The material, which sedimented through 1.74 M surcrose was analyzed in respect to the various marker enzymes and for proteolytic activity. Proteinase activity was found in the material obtained after digitonin treatment and step gradient centrifugation of mitochondria. This finding shows the occurrence of a proteinase in mitochondria; After fractionation of mitochondria into outer and inner membrane, intermembrane fraction and matrix, the proteinase could be localized exclusively in the inner mitochondrial membrane. A possible physiological function of the enzyme during the biosynthesis of inner membrane constituents is discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
2
pubmed:volume
91
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
171-8
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:year
1978
pubmed:articleTitle
The localization of an intracellular membrane-bound proteinase from rat liver.
pubmed:publicationType
Journal Article