chymotrypsinogen


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chymotrypsinogen

(ˌkaɪməʊtrɪpˈsɪnədʒɪn)
n
(Biochemistry) the inactive precursor of chymotrypsin
[C20: from chymotrypsin + -gen]
Translations

chy·mo·tryp·sin·o·gen

n. quimotripsinógeno, enzima pancreática precursora de la quimotripsina.
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has been granted US patent from the United States Patent and Trademark Office (USPTO) covering composition of matter claims involving trypsinogen and chymotrypsinogen. The additional composition claims are a continuation from the original foundation patent in the U.S., and as a result, both method of treatment and composition claims now protects the Company's lead product candidate, PRP, a pharmaceutical composition consisting of two proenzymes, trypinsogen and chymotrypsinogen, for treating cancer.
(OTC: PPCB) ('Propanc'), a biopharmaceutical company developing new cancer treatments for patients suffering from recurring and metastatic cancer, announced today that it has received a granted US patent from the United States Patent and Trademark Office (USPTO) covering composition of matter claims involving trypsinogen and chymotrypsinogen.
PRP is a mixture of two proenzymes, trypsinogen and chymotrypsinogen, administered by intravenous injection.
PRP is the mixture of two proenzymes (trypsinogen and chymotrypsinogen) from bovine pancreas.
Further, the late appearance of chymotrypsin seems to occur because the required levels of trypsin increased, in part, to hydrolyze proteins coming from food enabled zymogens of various enzymes, including chymotrypsinogen to be utilized (Jimenez-Martinez et al., 2012).
Several genetic mutations, including human cationic trypsinogen (PRSS) 1, PRSS2, serine protease inhibitor Kazal type 1 gene (SPINK1), chymotrypsinogen C gene (CTRC), transmembrane conductance regulator gene (CFTR), and calcium-sensing receptor (CASR), have been noted as risk factors [2, 6].
The free trypsin cleaves the remaining trypsinogen and chymotrypsinogen to its active form chymotrypsin.
The following standards from the Pharmacia protein standard kit (Pharmacia, NJ, USA) were applied to the column: blue dextran (2,000,000Da), thyroglobulin (669,000Da), ferritin (440,000Da), catalase (232,000Da), aldolase (158,000 Da), bovine serum albumin (67,000 Da), ovalbumin (43,000 Da), chymotrypsinogen A (25,000 Da) and ribonuclease A (13,700Da).
Thyroglobulin (669 kDa), catalase (232 kDa), bovine serum albumin (67 kDa), and chymotrypsinogen (25 kDa) were used as standard proteins for molecular mass estimation.