Human Pepsinogen I ELISA Kit

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

Pepsin is an enzyme with the main function of breaking down proteins into peptides in the stomach. Commonly known as a protease its molecular mass is approximately 35 kDa. This enzyme arises from its inactive precursor pepsinogen which activates in the acidic environment of the stomach. Expression predominantly occurs in the gastric chief cells. Pepsin remains a critical player in protein digestion with pepsin solutions often utilized for in vitro digestion studies.

Biological function summary

Pepsin fulfills an important role in the digestive process by breaking down larger protein molecules into smaller peptides facilitating nutrient absorption. It does not form part of a larger protein complex but operates independently within the gastric environment. Pepsin's enzymatic action targets specific peptide bonds ensuring efficient degradation of dietary proteins into absorbable forms. The specificity of its substrate binding ensures effective digestion and subsequent utilization of amino acids.

Pathways

Pepsin's activity integrates into proteolytic pathways particularly the catabolic processes in the gastrointestinal tract. It interacts with other digestive enzymes including trypsin and chymotrypsin which further hydrolyze peptides originated by pepsin. These interactions highlight its seamless fit in the digestive enzyme cascade optimized for effective protein turnover and nutrient release into the body. The pepsin pathway coordinates closely with the gastric and duodenal enzymatic processes.

Associated diseases and disorders

Conditions such as peptic ulcers and Zollinger-Ellison syndrome link closely with excessive or dysregulated pepsin activity. Increased pepsin secretion in response to elevated gastric acid levels contributes to the degradation of the stomach lining aggravating ulcer formation. Alcohol-induced gastric mucosal damage also associates with heightened pepsin activity. Dysfunctional interactions involving pepsin and other gastric enzymes such as pepsinogen underline the pathological implications within these disorders.