A.L. Farr's scientific contributions
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Publications (22)
Since 1922 when Wu proposed the use of the Folin phenol reagent for
the measurement of proteins (l), a number of modified analytical pro-
cedures ut.ilizing this reagent have been reported for the determination
of proteins in serum (2-G), in antigen-antibody precipitates (7-9), and
in insulin (10).
Although the reagent would seem to be recommended...
Citations
... Supernatants obtained in each step of mild acid treatment of ICWs were applied to a DEAE-cellulose column (5 ml bed volume) equilibrated with 5 mM Tris-HCl (pH 7.4), and the column was eluted in a stepwise manner with the same buffer containing 50, 150, 250, 350, and 500 mM NaCl, respectively. Each fraction (5 ml) was collected, and hexose and phosphorus in each fraction were determined by the phenol/H 2 SO 4 method and the method of Lowry et al. (1954), respectively. Fractions eluted at 250 mM NaCl were dialyzed and applied to a DEAE-Sepharose R column (2 × 10 cm) equilibrated with 5 mM Tris-HCl (pH 7.4), and the column was eluted with a linear gradient of NaCl (0-350 mM) in the same buffer. ...
... Protein concentrations in the unfermented and fermented buttermilk and soymilk were determined using the Lowry method [25]. Titratable acidity (TA) was calculated in terms of %age lactic acid, by titration of the test samples against 0.1 N NaOH solution using phenolphthalein as an indicator to allow the development of light pink color [26]. ...
... Biochemical analysis and proximate analysis were performed for the characterization of macroalgal biomass. Within the scope of biochemical analysis, the carbohydrate, lipid, and protein contents of macroalgae were determined using the phenol-sulfuric acid method [22], the Bligh and Dyer method [23], and the Lowry method [24], respectively. Glucose and bovine serum albumin were used as standards for the determination of carbohydrate and protein contents, respectively. ...
... Mitochondrial protein concentrations of iBAT were determined by Folin phenol method using bovine serum albumin as standard (Lowry et al., 1951). and goat anti-mouse IgG (1:5,000; ZSGB-BIO Co., Beijing, China). ...
... One unit of protease activity was calculated as the quantity of tyrosine (μmol) produced from casein by 1-mg enzyme per minute. Additionally, to standardize the monoculture system, the amount of protein was measured by the Lowry method using bovine serum albumin as a standard protein (Lowry et al., 1951). HPLC-UV-Vis produced by Shimadzu Corporation (the LC-10AD system, Japan) was performed to quantify fluorouracil in the supernatant of each vial during anaerobic digestion. ...
... The levels of hydrogen peroxide generation (Pick and Keisari 1981) and lipid peroxidation (Ohkawa et al. 1979), and the activity of alkaline phosphatase (Neumann and Van Vreedendaal 1967) were measured in gill tissues. Total protein contents were determined according to the method of Lowry et al (1951). ...
... The omission of protein content can hamper proper interpretation of the field bioaccumulation and biomagnification of specific emerging contaminants, which tend to be more protein associated rather than lipid associated or somewhere in between (e.g., numerous chemicals classified as per-/poly-fluoroalkyl substances (PFASs)). Various standard assays have been developed for protein quantification (Lowry et al. 1951;Bradford 1976;Smith et al. 1985) and may be adopted for avian B/BT tests. ...
... One unit of xylanase activity (U) is defined as the quantity of xylanase that releases 1 mol of xylose per mL of crude enzyme extract per minute. Protein content was determined according to [20]. Bovine serum albumin was used as a standard. ...
... Glutamic oxaloacetic transaminase (GOT) and glutamine pyruvic transaminase (GPT) were measured by the method of [21]. Proteins content was assayed using the Lowry et al. method [22] using bovine serum albumin (BSA) as standard protein, glycogen content and total lipids were measured by [23,24], respectively. ...
... Se utilizó el método colorimétrico propuesto por Lowry et al. (1951). Se agregaron 2 mL de NaOH 1 M a 10 mg de biomasa seca, las muestras se sometieron a baño de maría a 95-100 ºC por 1 hora y se dejaron enfriar a temperatura ambiente. ...