1985
DOI: 10.1007/bf02691582
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Reversible change in the fibroblast lysosomal enzyme dipeptidyl aminopeptidase-1 (cathepsin c) related to the commercial source of fetal bovine serum in the culture medium

Abstract: The commercial source of fetal bovine serum used to supplement the growth medium of human skin fibroblasts alters the activity of the lysosomal enzyme dipeptidyl aminopeptidase-1 (DAP-1). Cells grown with one serum were found to have a threefold higher level of DAP-1 than those grown with serum from another source (P less than 0.001). The effect on DAP-1 activity was specific inasmuch as no differences were found in the activities of a variety of other lysosomal and nonlysosomal hydrolases: DAP-II, DAP-III, DA… Show more

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Cited by 3 publications
(2 citation statements)
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“…The activity of hexosaminidase (Cabezas 1989) in the semm was determined following a previously published protocol (Doughty et al 1985;Doughty and Gmenstein 1988) using 4-methyl~kBliferyl-N-acety1-~-~)-gdactos~~de (M-9 129, Sigma) at pH 4.6 and 3'7°C. For the assays, 100 pL of a buffer solution (50 mM dimethylglutaric acid -NaOB; pH 4.6) was mixed with 100 pL of substrate solution (0.5 mM prepared in water), and 25 pL semm was added to start the reaction.…”
Section: Assessment Of Hemoglobin Content Of Serummentioning
confidence: 99%
“…The activity of hexosaminidase (Cabezas 1989) in the semm was determined following a previously published protocol (Doughty et al 1985;Doughty and Gmenstein 1988) using 4-methyl~kBliferyl-N-acety1-~-~)-gdactos~~de (M-9 129, Sigma) at pH 4.6 and 3'7°C. For the assays, 100 pL of a buffer solution (50 mM dimethylglutaric acid -NaOB; pH 4.6) was mixed with 100 pL of substrate solution (0.5 mM prepared in water), and 25 pL semm was added to start the reaction.…”
Section: Assessment Of Hemoglobin Content Of Serummentioning
confidence: 99%
“…The pellet (Pio.ooo; the crude mitochondriallysosome fraction) was resuspended in 1.5 ml of homo genisation buffer. Enzyme assays were performed in duplicate at 37°C for 30 min for hexosaminidase us ing 0.4 mM 4-methylumbelliferyl-N-acetyl-P-Z)-galactosaminide at pH 4.6 in 250 mM sucrose [6], acid phosphatase using 10 m.M /Miitrophcnyl phosphate at pH 4.0 in 250 mM sucrose [7], lactate dehydrogenase using 2 mV/ DL-lactate and 5 m M p-NADH at pH 7 [8] and leucine arylamidasc using 0.06 m M leucyl-2-naphthylamide at pH 7.5 in the presence of 0.1 mM C0CI2 [9]. The lysosomal enzyme activities in the Pio.ooo material were assessed with and without Triton X-100 detergent 0.02% w/v to assess latency [6]; the concentration of Triton X-100 was determined, from dose-response curves, to be non-inhibitory.…”
Section: Materials and M Ethodsmentioning
confidence: 99%