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Tan PS, Chapot-Chartier MP, Pos KM, et al. Localization of peptidases in lactococci. Appl Environ Microbiol. 1992;58(1):285-90doi: 10.1128/aem.58.1.285-290.1992.
Tan, P. S., Chapot-Chartier, M. P., Pos, K. M., Rousseau, M., Boquien, C. Y., Gripon, J. C., & Konings, W. N. (1992). Localization of peptidases in lactococci. Applied and environmental microbiology, 58(1), 285-90. https://doi.org/10.1128/aem.58.1.285-290.1992
Tan, P S, et al. "Localization of peptidases in lactococci." Applied and environmental microbiology vol. 58,1 (1992): 285-90. doi: https://doi.org/10.1128/aem.58.1.285-290.1992
Tan PS, Chapot-Chartier MP, Pos KM, Rousseau M, Boquien CY, Gripon JC, Konings WN. Localization of peptidases in lactococci. Appl Environ Microbiol. 1992 Jan;58(1):285-90. doi: 10.1128/aem.58.1.285-290.1992. PMID: 16348629; PMCID: PMC195205.
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Appl Environ Microbiol. 1992 Jan;58(1):285-90. doi: 10.1128/aem.58.1.285-290.1992.

Localization of peptidases in lactococci.

Applied and environmental microbiology

P S Tan, M P Chapot-Chartier, K M Pos, M Rousseau, C Y Boquien, J C Gripon, W N Konings

Affiliations

  1. Department of Microbiology, University of Groningen, Kerklaan 30, 9751 NN Haren, The Netherlands, and Station de Recherches Laitieres, Institute National de la Recherche Agronomique, 78350 Jouy-en-Josas, and Laboratoire de Génie des Procédés Biotechnologiques Agro-alimentaires, Institute National de la Recherche Agronomique, 7850 Thiverval-Grignon, France.

PMID: 16348629 PMCID: PMC195205 DOI: 10.1128/aem.58.1.285-290.1992

Abstract

The localization of two aminopeptidases, an X-prolyl-dipeptidyl aminopeptidase, an endopeptidase, and a tripeptidase in Lactococcus lactis was studied. Polyclonal antibodies raised against each purified peptidase are specific and do not cross-react with other peptidases. Experiments were performed by immunoblotting after cell fractionation and by electron microscopy of immunogold-labeled peptidases. All peptidases were found to be intracellular. However, immunogold studies showed a peripheral labeling of the X-prolyl-dipeptidyl aminopeptidase, the tripeptidase, and the endopeptidase. This peripheral location was further supported by the detection of these three enzymes in cell membrane fractions in which none of the two aminopeptidases was present.

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