Multiplicities and some enzymatic characteristics of ape pepsinogens and pepsins

Y Narita1, S Oda, O Takenaka

  • 1Laboratory of Animal Management, Nagoya University School of Bio-Agricultural Sciences, Japan.

Related Concept Videos

Protein Digestion01:31

Protein Digestion

Protein digestion begins in the stomach, where the highly acidic environment can easily disrupt protein structure by exposing the peptide bonds of polypeptide chains. After polypeptide chains are broken into individual amino acids by a series of digestive enzymes, the amino acids are transported to the liver via the bloodstream to produce energy.
Pancreatic Juice and Secretion01:26

Pancreatic Juice and Secretion

Pancreatic juice is a clear fluid produced by the pancreas, containing water, salts, sodium bicarbonate, and enzymes vital for digestion in the small intestine. It helps break down large molecules, facilitating nutrient absorption.
When acidic chyme from the stomach enters the duodenum, it triggers the release of secretin, a hormone that prompts pancreatic juice secretion. After a fatty meal, cholecystokinin, another hormone, stimulates gallbladder contraction and enhances enzyme-rich...
Proteins and Amino Acids02:17

Proteins and Amino Acids

Proteins are chains of amino acids that are connected by peptide bonds and folded into a 3-dimensional structure. The side chains of individual amino acid residues determine the interactions among amino acid residues, and ultimately the folding of the protein. Depending on the length and structural complexity, chains of amino acid residues are classified as oligopeptides, polypeptides, or proteins.Amino Acid Residues Are the Building Blocks of ProteinsAn amino acid is a molecule that contains a...
Enzymes02:34

Enzymes

Inside living organisms, enzymes act as catalysts for many biochemical reactions involved in cellular metabolism. The role of enzymes is to reduce the activation energies of biochemical reactions by forming complexes with its substrates. The lowering of activation energies favor an increase in the rates of biochemical reactions.
Enzyme deficiencies can often translate into life-threatening diseases. For example, a genetic abnormality resulting in the deficiency of the enzyme G6PD...
Cholinesterases: Distribution and Function01:22

Cholinesterases: Distribution and Function

Cholinesterases are a group of serine hydrolase enzymes that play a crucial role in the breakdown of choline esters. The two primary types of cholinesterases are acetylcholinesterases (AChEs) and butyrylcholinesterase (BuChEs), which differ in their distribution, function, and substrate specificity. AChEs, also known as true cholinesterases, specifically hydrolyze acetylcholine, while BuChEs, often referred to as pseudocholinesterases, can hydrolyze various choline esters, including...
Catalytically Perfect Enzymes01:07

Catalytically Perfect Enzymes

The theory of catalytically perfect enzymes was first proposed by W.J. Albery and J. R. Knowles in 1976. These enzymes catalyze biochemical reactions at high-speed. Their catalytic efficiency values range from 108-109 M-1s-1. These enzymes are also called 'diffusion-controlled' as the only rate-limiting step in the catalysis is that of the substrate diffusion into the active site. Examples include triose phosphate isomerase, fumarase, and superoxide dismutase.