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ENDOGENOUS INCORPORATION OF 32 P IN NEISSERIA MENINGITIDIS
Author(s) -
Jyssum Sidsel,
Jyssum Kaare
Publication year - 1970
Publication title -
acta pathologica microbiologica scandinavica section b microbiology and immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.909
H-Index - 88
eISSN - 1600-0463
pISSN - 0365-5563
DOI - 10.1111/j.1699-0463.1970.tb04312.x
Subject(s) - phosphorylation , oxidative phosphorylation , endogeny , neisseria meningitidis , chemistry , biochemistry , cytochrome c oxidase , electron transport chain , oxidase test , enzyme , biology , bacteria , genetics
Meningococcal extracts mediate an incorporation of 32 P in the presence of Mg 44 and ADP which is improved by the addition of EDTA. A major part of this incorporation is due to a polynucleotide phosphorylase activity, and is independent of electron flux. But the endogenous respiration is also accompanied by a phosphorylation. When the cytochrome oxidase is inhibited by KCN phosphorylation occurs concomitantly with the endogenous reduction of added mammalian ferricytochrome c. This phosphorylation is nearly doubled when KHCO 3 is included in the system. It has not been possible to demonstrate an oxidative phosphorylation on the electron‐oxygen transport level in meningococcal extracts with NADH, NADPH or ferrocytochrome c as electron sources. The phosphorylation connected with electron flux, and its enhancement by KHCO 3 have been discussed in relation to the CO 2 requirements typical for N. meningitidis.