Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1980-11-25
pubmed:abstractText
The intracellular localization of two forms of membrane-bound acid protease (M1 and M2) [EC 3.4.23.6] of Aspergillus oryzae (Tsujita, Y. & Endo, A. (1978) Eur. J. Biochem. 84, 347-353) was investigated. When the mycelia were treated with wall-lytic enzymes, M2 remained in the cells but most of M2 was solubilized and released. The cell wall fraction obtained by mechanical disruption of the mycelia contained less than 5% of the total acid protease activity in the cells. Subcellular fractionation of the membranes obtained from burst spheroplasts showed that the acid protease was present in both rough and smooth microsomes. Acid protease M1 was predominant in the former and M2 in the latter, possibly on the surface of the cytoplasmic membranes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0021-924X
pubmed:author
pubmed:issnType
Print
pubmed:volume
88
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
113-20
pubmed:dateRevised
2007-12-19
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
Intracellular localization of two molecular forms of membrane acid protease in Aspergillus oryzae.
pubmed:publicationType
Journal Article