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Leu gly pro ala

Manufactured by Merck Group
Sourced in France

Leu-Gly Pro-Ala is a tetrapeptide composed of the amino acids leucine, glycine, proline, and alanine. It is commonly used in laboratory research as a biochemical standard or reference material.

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3 protocols using leu gly pro ala

1

Collagenase Activity Assay Protocol

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Collagenase from Clostridium histolyticum (Sigma Aldrich, Saint Quentin Fallavier, France) was used. The collagenase activity was determined using N-[3-(2-furyl) acryloyl]-Leu-Gly Pro-Ala (FALGPA; Sigma Aldrich, Saint Quentin Fallavier, France) as a substrate following the protocol of Wittenauer et al. [34 (link)]. Absorbance decrease was followed at 335 nm during 20 min thank to a microplate reader (BioTek ELX800; BioTek Instruments, Colmar, France). The collagenase activity in presence of each extraction conditions was determined in triplicated and the anti-collagenase activity was expressed, for each extract, as an inhibition percentage relative to corresponding control (adding same volume of extraction solvent).
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2

Collagenase Inhibition Assay Protocol

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Collagenase clostridium histolyticum (Sigma Aldrich) was employed for this assay and its activity was determined with the aid of a spectrophotometer by making use of N-[3-(2-furyl)acryloyl]-Leu-Gly-Pro-Ala (FALGPA; Sigma Aldrich) as a substrate in accordance to the protocol of Wittenauer et al. (2015) [78 (link)]. The absorbance decrease of FALGPA was followed at 335 nm for 20 min using a microplate reader (BioTek ELX800; BioTek Instruments, Colmar, France). Triplicated measurements were used and the anti-collagenase activity was revealed as a % of inhibition relative to corresponding control (adding same volume of extraction solvent) for every extract.
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3

Collagenase Activity Assay Protocol

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Collagenase clostridium histolyticum (Sigma Aldrich) was used for this experiment, and its activity was determined with the aid of a spectrophotometer using N-[3-(2-furyl)acryloyl]-Leu-Gly-Pro-Ala (FALGPA; Sigma Aldrich) as the substrate in accordance with the protocol of Wittenauer et al. [51 (link)]. The decrease in the absorbance of the FALGPA was followed for 20 min at 335 nm using a microplate reader (BioTek ELX800; BioTek Instruments, Colmar, France). The measurements were conducted in triplicate, and the anti-collagenase activity was revealed as the percent inhibition relative to the control (extraction solvent) for every extract sample. 1,10-Phenantroline (100 µM) was used as the specific inhibitor of collagenase.
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