Localization of proteinase(s) near the cell surface of Streptococcus lactis.
Two criteria suggest that most of the proteinase of Streptococcus lactis is localized in the cell wall. (i) Intact cells possess proteinase activity when incubated with a high-molecular-weight substrate. (ii) Most of the cell-bound proteinase activity is released during spheroplast formation under conditions which result in the release of only 1% of the intracellular enzymes aldolase and glyceraldehyde-3-phosphate dehydrogenase. The solubilized cell wall, plasma membrane, and cytoplasm fractions contained 84, 0, and 16%, respectively, of the total proteinase activity with casein as substrate. The physiological role of a surface-bound proteinase in this organism is discussed.
D002364:Caseins / Q000378:metabolism; D002458:Cell Fractionation; D002462:Cell Membrane / Q000201:enzymology; D002473:Cell Wall / Q000201:enzymology; D002474:Cell-Free System; D003593:Cytoplasm / Q000201:enzymology; D005634:Fructose-Bisphosphate Aldolase / Q000378:metabolism; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000378:metabolism; D007457:Iodine Radioisotopes; D013294:Lactococcus lactis / Q000201:enzymology*; D010447:Peptide Hydrolases / Q000302:isolation & purification* / Q000378:metabolism; D013104:Spheroplasts / Q000302:isolation & purification
D002364:Caseins; D007457:Iodine Radioisotopes; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D010447:Peptide Hydrolases; D005634:Fructose-Bisphosphate Aldolase