Localization of enzymes in Ureaplasma urealyticum (T-strain mycoplasma).

Abstract:

:Ureaplasma urealyticum cells were lysed by osmotic shock or by digitonin. The membrane fraction contained four to ten times as much protein as the cytoplasmic fraction. These values are in large excess of those reported for classical mycoplasmas, suggesting that the Ureaplasma membrane fraction was heavily contaminated with proteins derived from the growth medium. The U. urealyticum urease activity was localized in the cytoplasmic fraction, whereas the adenosine triphosphatase activity was localized in the membrane fraction. Significant urease activity could be detected also in nonviable cells. Urea, at concentrations above 0.25 M, was mycoplasmastatic to Acholeplasma laidlawii, Mycoplasma hominis, and U. urealyticum, so that the Ureaplasma urease did not afford preferential protection against urea toxicity. The intracellular localization of the urease would be expected to release ammonia from urea in the cytoplasm. The ammonia will take up protons to become ammonium ions. It can be hypothesized that the intracellular NH4+ plays a role in proton elimination or acid-base balance, which might be coupled to an energy producing ion gradient and/or transport mechanisms.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Masover GK,Razin S,Hayflick L

doi

10.1128/JB.130.1.297-302.1977

keywords:

subject

Has Abstract

pub_date

1977-04-01 00:00:00

pages

297-302

issue

1

eissn

0021-9193

issn

1098-5530

journal_volume

130

pub_type

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