The Colorimetric Determination of Lipase and Esterase in Human Serum 1

Seligman, Arnold M.; Nachlas, Marvin M.

doi:10.1172/jci102231

Cited by 118 publications

(20 citation statements)

References 7 publications

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“…The amylase method used is not highly accurate and the esterase method, although it gave accurately reproducible results, measures anything in the serum that can split phenylbenzoate. The amount of splitting performed by lipase is undetermined; it is in fact considered doubtful if serum contains any lipase at all (Seligman & Nachlas, 1950). In spite of these uncertainties, the curves obtained for amylase and esterase activity demonstrated the recovery of enzyme systems as treatment progressed.…”

Section: Discussionmentioning

confidence: 99%

The Serum Chemistry in Uncomplicated Kwashiorkor

1953

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Section: Discussionmentioning

confidence: 99%

The Serum Chemistry in Uncomplicated Kwashiorkor

1953

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“…Acid phosphatase: Assays were performed using a modification of the method of Seligman et al (22). 2 ml of the substrate ~-naphthol acid phosphate (0.2 mg in 0.1 ~ acetate buffer, pH 5.0) were added to 1.0 ml of frozen-thawed cells and the mixture incubated for 2 hours at 37°C with occasional shaking.…”

Section: T Flasksmentioning

confidence: 99%

The Isolation and Selected Properties of Blood Monocytes

Bennett

Cohn

1966

The Journal of Experimental Medicine

282

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A technique is described for the quantitative recovery of monocytes from horse blood by means of flotation on dense albumin solutions. Monocytes are concentrated in a surface pellicle along with a few lymphocytes which are then removed when the monocytes adhere to a glass surface. The in vitro cultivation of homogeneous populations of monocytes results in an increase in (a) cell size, (b) number of mitochondria, and (c) phase-dense granules of the centrosphere. The phase-dense granules are osmiophilic and acid phosphatase positive. Quantitative biochemical analysis during cultivation have revealed increased levels of cytochrome oxidase, acid phosphatase, arylsulfatase, and BPN hydrolase. In addition, glucose utilization and lactic acid production are stimulated under the same conditions. The uptake of both bacteria and colloidal gold is stimulated during in vitro cultivation. The phagocytic activity of cultured monocytes may be enhanced by a purified bacterial lipopolysaccharide. These data are consistant with the in vitro maturation of monocytes to macrophages, a cell with greater metabolic and functional potentional.

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“…The acceptor of liberated fatty acids was delipidized bovine albumin [15]. The /S-naphthol released from the /S-naphthylesters was determined according to Seligman and N achlas [9], One enzyme unit (U) is the amount of activity that released 1 //mol naphthol/min. Protein was assayed by the biuret reaction.…”

Section: Methodsmentioning

confidence: 99%

“…Tween 20, 40 and 60 were dispersed in deionized water (final concentration 11.2 mM). The /J-naphthylesters of fatty acids were dissolved as previously shown [9]. Identification and determination of the reaction products.…”

Section: Methodsmentioning

confidence: 99%

Triglyceride Lipase Activity in Bovine Aorta

Filipović¹,

Rutemöller²,

Helten³

1975

J Vasc Res

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The cell-free supernatant from homogenized bovine aorta hydrolyzed triglycerides, β-naphthylesters of lauric and stearic acid and Tween 20, 40 and 60. The rate of hydrolysis decreases as the acyl chain length of the substrates increases. The activity against triglycerides of short-chain fatty acids and monoacylesters could be partially separated from that of glycerol-trioleate lipase by ammonium sulfate fractionation. The activity of glycerol-trioleate lipase remained unaffected by heating for 5 min at 60 °C or by addition of bile acids, whereas the activity causing hydrolysis of triglycerides with short-chain fatty acids and monoacylesters decreases up to 60% by analogous treatment. No changes in the hydrolytic activity occurs in presence of sodium heparin. This indicates that this activity is not identical with a lipoprotein lipase.

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The Colorimetric Determination of Lipase and Esterase in Human Serum 1

Cited by 118 publications

References 7 publications

The Serum Chemistry in Uncomplicated Kwashiorkor

The Serum Chemistry in Uncomplicated Kwashiorkor

The Isolation and Selected Properties of Blood Monocytes

Triglyceride Lipase Activity in Bovine Aorta

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