Trypsin

... to glucose and galactose Protein Enzymes Pepsin (secreted as pepsinogen) - made in gastric glands, functions in the stomach to break peptide bonds Trypsin (secreted as trypsinogen) - made in pancreas, functions in the small intestine to break specific peptide bonds and converts chymotrypsinogen ...

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... we have a picture of a ladder starting from 10kD up till 250kD and next to it it has a bunch of proteins such as albumin from bovie 66000Da and Trypsin Inhibitor from soybean 20100Da. It then goes on to say make a plot of log (molecular weight) against relative mobility for each standard protein. ...

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... that proteases refers to a large group of enzymes - each of which has a specificity - based on amino acid sequence, charge, size, etc. For example trypsin cleaves peptide chains at the carboxyl side of the amino acids lysine and arginine, except when either is followed by proline. The "lipase" ...

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... Here's why it's important: http://www.molecularstation.com/forum/cell-biology-cell-culture/2883-function-edta-trypsin.html

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Just google "trypsinization" and you will get most of the information you want to know. EDTA is a standard chelator of (forms a soluble complex with) calcium and magnesium ions, both of which inhibit the enzyme trypsin. Cells ...

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