Volume 11, Issue 3 (October 2004)
J Birjand Univ Med Sci. 2004, 11(3): 5-11 |
Back to browse issues page
Download citation:
BibTeX | RIS | EndNote | Medlars | ProCite | Reference Manager | RefWorks
Send citation to:
BibTeX | RIS | EndNote | Medlars | ProCite | Reference Manager | RefWorks
Send citation to:
Rajabi O, Varaste A, Danaee Baghaki J, Baratian A, Jahangiri L. جداسازی و تعیین خواص چهار پروتئاز جدا شده از لاتکس درخت انجیر بومی خراسان (Ficus Carica. J Birjand Univ Med Sci. 2004; 11 (3) :5-11
URL: http://journal.bums.ac.ir/article-1-216-en.html
URL: http://journal.bums.ac.ir/article-1-216-en.html
1- Assistant Professor, Department of Medicinal Chemistry, Faculty of Pharmacy, Mashhad University of Medical Sciences, Mashhad, Iran
Abstract: (18293 Views)
Background and Aim: The protease activity of fig latex has been reported in several articles. This study was carried out aiming at a comparison between proteases of the latex of Khorasan native fig tree and those of carica subspecies.
Materials and Methods: In this experimental study, four latex proteases (Ficins) were extracted using salt fractionation and chromatography on Mono-S column (Ion exchange media). Parameters such as activity, concentration and molar extinction coefficient were determined at least 3 times per sample. The different samples were compared according to activity and molar extinction coefficient, using ANOVA statistical analysis. P<0.05 was taken as significant.
Results: These proteases were similar with regard to molar extinction coefficient, activity and molecular weight. Activity and molecular weight were determined by cosein perpetration and SDSPAGE respectively. Besides, the enzymes showed different properties as to retention time on cation exchanging column. This is supposed to be because of little differences in their primary structures and peptide maps. Protein concentration and the activity of latex was calculated to be 110 (mg/ml) and 242 (IU/ml) respectively. Agents having enzymatic activity were found in fraction III-VI. Molecular weight of Ficins III- VI was stimated at about 26.5- 121. A 1% solution of proteins of Fractions III- VI in 0.05 M NH4CO3 had a molar absorption coefficient (ε280 nm) of about 22, 21. 5, 21, 21.9 respectively. Enzymatic activity of Ficins (fractions III-VI) using casein substrate was 61.6, 62.7, 63.4 and 67.2 (unit/mol) respectively.
Conclusion: According to this study, latex of Khorasan native Fig tree is relatively similar to Calimyrna subspecies growing in California/USA among the four subspecies
Materials and Methods: In this experimental study, four latex proteases (Ficins) were extracted using salt fractionation and chromatography on Mono-S column (Ion exchange media). Parameters such as activity, concentration and molar extinction coefficient were determined at least 3 times per sample. The different samples were compared according to activity and molar extinction coefficient, using ANOVA statistical analysis. P<0.05 was taken as significant.
Results: These proteases were similar with regard to molar extinction coefficient, activity and molecular weight. Activity and molecular weight were determined by cosein perpetration and SDSPAGE respectively. Besides, the enzymes showed different properties as to retention time on cation exchanging column. This is supposed to be because of little differences in their primary structures and peptide maps. Protein concentration and the activity of latex was calculated to be 110 (mg/ml) and 242 (IU/ml) respectively. Agents having enzymatic activity were found in fraction III-VI. Molecular weight of Ficins III- VI was stimated at about 26.5- 121. A 1% solution of proteins of Fractions III- VI in 0.05 M NH4CO3 had a molar absorption coefficient (ε280 nm) of about 22, 21. 5, 21, 21.9 respectively. Enzymatic activity of Ficins (fractions III-VI) using casein substrate was 61.6, 62.7, 63.4 and 67.2 (unit/mol) respectively.
Conclusion: According to this study, latex of Khorasan native Fig tree is relatively similar to Calimyrna subspecies growing in California/USA among the four subspecies
Type of Study: Original Article |
Subject:
Biochemistry
Received: 2006/09/6 | Accepted: 2014/01/9 | ePublished: 2014/01/9
Received: 2006/09/6 | Accepted: 2014/01/9 | ePublished: 2014/01/9
| Rights and permissions | |
 |
This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License. |
Attribution-NoneCommercial CC BY-NC