Respuesta :
Scientists originally hypothesized that proteolytic enzymes such as pepsin and trypsin are secreted in inactive form because these proteolytic enzymes, in active form, would digest the very tissues that synthesize them.
Pepsin is a proteolytic enzyme that is made by the chief cells of the stomach. Trypsin is another proteolytic enzyme that is formed by the pancreas and brought to the small intestine at the time of digestion.
The chief cells form pepsin originally as pepsinogen. The pancreas secretes trypsin originally as trypsinogen. As there are various proteins that are present in the chief cells as well as the pancreas, hence making of these enzymes would mean that they will break down the other enzymes and proteins of the very own cells that created them.
Hence, pepsin and trypsin are formed in their inactive forms and are only converted into their active forms at the time of digestion.
Although a part of your question is missing, you might be referring to this question:
Why did scientists originally hypothesize that proteolytic enzymes such as pepsin and trypsin are secreted in inactive form?
A) These proteolytic enzymes, in active form, would digest the very tissues that synthesize them.
B) They identified the hormone that activates pepsin and trypsin.
C) The stomach is too acidic to maintain these enzymes in their active form.
D) Pepsin and trypsin have never been isolated in their fully activated form.
To learn more about proteolytic enzymes, click here:
https://brainly.com/question/13735056
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