Chymotrypsin

Next, the smaller proteins move into the small intestine, where pancreatic enzymes, trypsin and chymotrypsin, continue the breakdown of proteins into amino acids. ❋ M.S. Carrie Wiatt (2011)

Northrop, however, managed to crystalize three digestive enzymes, pepsin, trypsin and chymotrypsin, and by painstaking experiments shown them to be pure proteins. ❋ Unknown (2010)

Proteinase inhibitors, affecting trypsin and chymotrypsin, have been found in seeds of A. cowleana and other species. but only at levels similar to those found in peas or beans-much lower than levels in soybeans or winged beans (Kortt, 1984). ❋ Unknown (1990)

In 1929 he isolated pepsin in pure crystalline form by techniques which were later used by himself and other workers to crystallize trypsin, chymotrypsin, carboxypeptidase, and pepsinogen. ❋ Unknown (1964)

Princeton began to work on the purification of the protein-splitting enzymes met with in the digestive apparatus and gradually succeeded in obtaining a number of them in crystallized form, e.g. the pepsin met with in the gastric juice and the trypsin and chymotrypsin in the pancreas. ❋ Unknown (1964)

The chymotrypsin crystals were twinned and therefore difficult to work with, and so Perutz continued with haemoglobin. ❋ Unknown (1964)

Bernal, Fankuchen, and Perutz [Nature, 141 (1938) 523] published a joint paper on X-ray diffraction from crystals of haemoglobin and chymotrypsin. ❋ Unknown (1964)

Proteases, trypsin and chymotrypsin, are used to break down proteins. ❋ Unknown (2010)

Trypsin and chymotrypsin are usually inactive when they are not at work, therefore, they are treated as hazardous or troubling enzymes. ❋ Unknown (2010)

The most frequently used biological molecules included in the digestion models were digestive enzymes (pancreatin, pepsin, trypsin, chymotrypsin, peptidase, α-amylase, and lipase), bile salts, and mucin. ❋ Unknown (2010)

First, we investigated the consequences of moisture sorption on the stability and structural conformation of the model enzyme alpha-chymotrypsin (alpha-CT) under controlled humidity conditions. ❋ Unknown (2010)

Samples were subjected to reduction with dithiothreitol, alkylation with iodoacetamide, and in-gel digestion with trypsin or chymotrypsin overnight at pH 8.3, followed by reversed-phase microcapillary/tandem mass spectrometry (LC/MS/MS). ❋ Dana M. Gwinn Et Al. (2010)

Both recombinant human enzymes were nitrated in vitro with SIN-1 and digested with trypsin and chymotrypsin. ❋ Alfredo Csibi Et Al. (2010)

Proteases, trypsin and chymotrypsin, are used in reducing the size or volume of protein in the body. ❋ Unknown (2010)