Sidenote: Comparison of trypsin and pepsin] The second enzym to be considered in the pancreatic juice is trypsin.
A number of forms of proteid that are not acted on at all by the gastric juice are readily digested by the trypsin of the pancreatic juice.
Trypsin is much more energetic in its digestive power than the pepsin of the gastric juice.
The chief distinction is that trypsin acts in an alkaline solution, while pepsin acts in an acid solution.
The direct action of commercial trypsin on boiled yeast-juice also yielded [p068] a negative result, although this cannot strictly be regarded as an indication of the effect of the specific proteoclastic enzymes of yeast-juice.
The lipase of castor oil seeds, a glycerol extract of the intestinal mucous membrane of the rabbit and pig, and an aqueous extract of bran have a slow hydrolytic action, whereas pepsin and trypsin are without effect.
My work was undertaken solely out of interest to see whether trypsin could exist in the powder (which gives a markedly acid solution when dissolved in water).
Balch’s result for trypsin or rennin as reliable.
Hawk and Benedict show a degree of tryptic activity which, though chemically not negligible, is quite without significance practically, even if it could be assumed that the trypsin in the fresh Lactopeptine escaped destruction in the stomach.
Defn: Relating to trypsin or to its action; produced by trypsin; as, trypsin digestion.
It is digested by trypsin and slowly destroyed by the fat solvent anaesthetics, such as chloroform.
Why, for example, does pepsin act on proteid matter only in the presence of acid, and trypsin to advantage only in the presence of alkalies?
Furthermore, pepsin is limited in its action to the production of proteoses and peptones, while trypsin gives rise to a series of hydrolytic cleavages which result in the ultimate formation of comparatively simple bodies.
In general properties and reactions, pepsin and trypsin may be closely related; both are products of the katabolic action of specific protoplasmic cells, but the inner nature or structure of the two must be quite different.
Similarly, the products of pepsin-proteolysis exposed to the action of trypsin may undergo a like separation, the hemi-groups only breaking down into simple products.
The power of the ferment as a contact agent is astonishing, for in the case of trypsin no accessory body is necessary to bring out its latent power.
Such a peptone exposed to the proteolytic action of trypsin should obviously break down in part into simple crystalline bodies, leaving a residue of true antipeptone.
With the purer preparations now obtainable there is apparently less coagulable matter present, and Loew[31] has succeeded in preparing from the pancreas of the ox a sample of trypsin containing 52.
Gastric digestion is to be considered rather as a preliminary step in proteolysis, preparatory to the more profound changes characteristic of pancreatic digestion, in which the ferment trypsin is the important factor.
Why does trypsin produce a different set of soluble products in the digestion of albumin than pepsin does?
The above list will hopefully give you a few useful examples demonstrating the appropriate usage of "trypsin" in a variety of sentences. We hope that you will now be able to make sentences using this word.
