F4165
Ficin from fig tree latex
powder, ≥0.1 unit/mg solid
Synonym(s):
Debricin, Ficain, higueroxyl delabarre
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About This Item
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biological source
fig tree (latex)
form
powder
specific activity
≥0.1 unit/mg solid
mol wt
23.8 kDa
storage temp.
−20°C
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General description
Extinction Coefficient: E1% = 21.0 (280 nm)
pI: 9.0
pI: 9.0
Biochem/physiol Actions
Ficin is classified as a thiol protease. It contains a single reactive cysteine at its active site. The amino acid homology of the active site is similar to that of papain. Ficin will cleave proteins at the carboxyl side of Gly, Ser, Thr, Met, Lys, Arg, Tyr, Ala, Asn, and Val. The reported Km for the chromogenic substrate pGlu-Phe-Leu-p-nitroanilide is 0.43 mM. Ficin is inhibited by iodoacetamide, iodoacetic acid, N-ethylmaleimide, mercuric chloride, DFP (diisopropyl fluorophosphate), TLCK (Na-p-Tosyl-lysine chloromethyl ketone), and TPCK (N-Tosyl-L-phenylalanine chloromethyl ketone). Ficin can be used to generate high yielding F (ab′)2 fragments from mouse IgG1.
Unit Definition
One unit will produce a ΔA280 of 1.0 per min at pH 7.0 at 37 °C when measuring TCA soluble products from casein in a final volume of 10 ml (1 cm light path).
The enzyme is soluble in 1 M potassium phosphate buffer, pH 7.0 (0.25 mg/ml), yielding a clear solution.
inhibitor
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Description
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substrate
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Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
Target Organs
Respiratory system
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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Yufang Yang et al.
Scientific reports, 7, 43141-43141 (2017-02-23)
Ficin is classified as a sulfhydryl protease isolated from the latex of fig trees. In most cases, a particular enzyme fits a few types of substrate and catalyzes one type of reaction. In this investigation, we found sufficient proofs for
K B Devaraj et al.
International journal of biological macromolecules, 45(3), 248-254 (2009-06-02)
Effect of pH on the conformational behaviour of ficin (EC 3.4.22.3), a cysteine protease from the latex of Ficus carica was monitored by circular dichroism, fluorescence spectroscopy, ANS binding and hydrodynamic studies. The results obtained from near- and far-UV CD
Michèle Himmelspach et al.
Thrombosis and haemostasis, 88(6), 1003-1011 (2003-01-17)
The development of inhibitory antibodies is a serious complication in hemophilic patients, severely compromising therapeutic success. Bleeding episodes in affected patients are controlled by treatment with a plasma-derived prothrombin complex concentrate (PCC), activated PCC (APCC) or recombinant activated factor VII.
J D Reid et al.
The Biochemical journal, 357(Pt 2), 343-352 (2001-07-06)
The possibility of a slow post-acylation conformational change during catalysis by cysteine proteinases was investigated by using a new chromogenic substrate, N-acetyl-Phe-Gly methyl thionoester, four natural variants (papain, caricain, actinidin and ficin), and stopped-flow spectral analysis to monitor the pre-steady
Sadami Ohtsubo et al.
Journal of agricultural and food chemistry, 53(13), 5218-5224 (2005-06-23)
On the basis of cDNA sequences, we found that the calli of rice encodes an amino acid sequence that shares 56% and 89% identity, respectively, with oryzacystatin-I and oryzacystatin-II. This sequence differs from that of oryzacystatin-II in the N-terminal region
Protocols
This procedure may be used for all Ficin products.
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