... figs contain ficain, and papaya contains papain. Cooking or canning denatures and deactivates the proteases, so canned ...
... s may be used for tenderizing meat in a manner similar to widely used tenderizers papain, bromelain and ficain. ...
... or the cells can be treated with enzymes such as ficain or papain which inhibit the reactivity of some blood group antibodies ... and enhance others.:723-9 The effect of ficain and papain on major blood group systems is as follows: Enhanced: ABO, Rh, Kidd, ...
When the wasp dies, it is broken down by enzymes (Ficain) inside the fig. Fig wasps are not known to transmit any diseases ...
The fig actually produces an enzyme called ficain (also known as ficin) which digests the dead wasps and the fig absorbs the ...
... amine gamma-glutamyl transferase Boneless Fish Surimi Bromelain Papain Ficain DeJong GA, Koppelman SJ (2002). "Transglutaminase ...
... ficain MeSH D08.811.277.656.300.215.585 - papain MeSH D08.811.277.656.300.480 - metalloendopeptidases MeSH D08.811.277.656. ...
... ficain EC 3.4.22.4: bromelain (stem). Now EC 3.4.22.32 (stem bromelain) and EC 3.4.22.33 (fruit bromelain) EC 3.4.22.5: ...
... (EC 3.4.22.3 debricin, higueroxyl delabarre), also spelled ficin, is an enzyme derived from figs latex. It is of a ... Ficain at the US National Library of Medicine Medical Subject Headings (MeSH) EC 3.4.22.3 Biology portal v t e. ...
... is a protein that in humans is encoded by the CTSW gene.[5][6][7]. The protein encoded by this gene, a member of the peptidase C1 family, is a cysteine proteinase that may have a specific function in the mechanism or regulation of T-cell cytolytic activity. The encoded protein is found associated with the membrane inside the endoplasmic reticulum of natural killer and cytotoxic T-cells. Expression of this gene is up-regulated by interleukin-2.[7]. ...
... s (cysteine-aspartic proteases, cysteine aspartases or cysteine-dependent aspartate-directed proteases) are a family of protease enzymes playing essential roles in programmed cell death (including apoptosis, pyroptosis and necroptosis) and inflammation. They are named caspases due to their specific cysteine protease activity - a cysteine in its active site nucleophilically attacks and cleaves a target protein only after an aspartic acid residue. As of 2009, there are 11 or 12 confirmed caspases in humans[note 1] and 10 in mice, carrying out a variety of cellular functions.. The role of these enzymes in programmed cell death was first identified in 1993, with their functions in apoptosis well characterised. This is a form of programmed cell death, occurring widely during development, and throughout life to maintain cell homeostasis. Activation of Caspases ensures that the cellular components are degraded in a controlled manner, carrying out cell death with minimal effect on surrounding ...
A very rare genetic disorder of the immune system can also be caused by mutations in this gene. This disease, called CEDS, stands for "Caspase eight deficiency state." CEDS has features similar to ALPS, another genetic disease of apoptosis, with the addition of an immunodeficient phenotype. Thus, the clinical manifestations include splenomegaly and lymphadenopathy, in addition to recurrent sinopulmonary infections, recurrent mucocutaneous herpesvirus, persistent warts and molluscum contagiosum infections, and hypogammaglobulinemia. There is sometimes lymphocytic infiltrative disease in parenchymal organs, but autoimmunity is minimal and lymphoma has not been observed in the CEDS patients. CEDS is inherited in an autosomal recessive manner.[7]. The clinical phenotype of CEDS patients represented a paradox since caspase-8 was considered to be chiefly a proapoptotic protease, that was mainly involved in signal transduction from Tumor necrosis factor receptor family death receptors such as Fas. The ...
... was first purified and characterized with X-ray crystallography in 2000 by researchers at Boston University.[1] The enzyme is 221 amino acids long and glycosylated with 2 N-linked oligosaccharide chains at Asn96 and Asn154.[3] The polypeptide chain of zingibain folds into two polar domains of roughly equal size, divided by a central neutral cleft.[3] The first domain contains alpha helices, and the second has antiparallel beta sheets.[3] This separation of polar and non-polar regions facilitates protein-protein interactions between the enzyme and a large range of substrates.[3] The active site of zingibain, located in the central cleft, is 5.5 Å deep and 9.5 Å long.[3] The active site contains the catalytic triad of Cys25, His159, and Asn175, which both cooperatively enable acid/base catalysis. Zingibain exhibits binding specificity to peptide substrates with proline in the P2 position.[1] The S2 subsite of zingibain contains the amino acid chain Trp67-Met68-Asn69-Thr133-Ala157, ...