Biochemistry

The catalysts can be used to increase or decrease the speed of a chemical reaction. The catalysts which reduce the speed of a reaction are called negative catalysts. They decrease the speed of the reaction by increasing the activation energy of the reaction.

Vitamin B-6 removes a carbon in chemical reactions. This gives it a role as an enzyme in over 100 reactions in the body. Some specific functions are carbohydrate metabolism, lipid metabolism, protein metabolism, neurotransmitter synthesis, and amino acid conversion/rearrangement.

Isoelectric pH, often referred to as the pI (isoelectric point), is the pH at which a molecule or substance carries no net electrical charge. It is the pH at which the molecule is neutral or balanced between positive and negative charges. At the isoelectric pH, the molecule tends to be least soluble in water due to its minimum ionization state.

Enzymes reduce the activation energy of a reaction. They accomplish this feat by altering the local chemical environment of the substrates while typically bringing the reactants into close proximity and even stabilizing conformers that promote reaction.

Iodine can react with lipid molecules by forming iodolipids, where the iodine molecule is bound to the lipid. This process is often used to detect the presence of lipids in a sample through a staining reaction called the iodine value test. This reaction helps to visualize the lipid molecules and is commonly used in food science and biochemistry.

A tungsten lamp is commonly used in a spectrophotometer as a light source due to its broad and continuous spectrum that covers the visible and near-infrared range. Additionally, deuterium lamps are often utilized for ultraviolet wavelengths in spectrophotometers.

No, they are not the same. Dendron refers to the main projection of a nerve cell, while dendrite is a smaller branch extending from the dendron that receives signals from other nerve cells.

A peptide bond is broken by hydrolysis, where a water molecule is used to break the bond between the amino acids in the peptide chain. This process involves the addition of a water molecule which leads to the separation of the amino acids.

Adding glucose to the starch hydrolysis medium would provide an additional readily available source of energy for the organisms present. This could potentially increase the growth rate and metabolism of those organisms, leading to a faster breakdown of starch into glucose. As a result, the rate of starch hydrolysis may be accelerated in the presence of glucose.

A liquid with a pH of 6 is considered slightly acidic. Examples include milk and urine.

The buffer system in blood is formed by carbonic acid (H2CO3) and bicarbonate ions (HCO3-). This system helps maintain the pH of blood within a narrow range by absorbing or releasing hydrogen ions as needed.

Horses and donkeys share a common ancestor, which is why their DNA sequences are similar. Although they belong to different species, they are part of the same genus (Equus), which explains the genetic resemblance between the two animals.

Flame photometry is used in biological samples for measuring the concentration of ions like sodium, potassium, calcium, and magnesium. It provides a rapid and accurate method for detecting the presence of these ions in samples such as blood, urine, and tissue extracts. This technique plays a crucial role in diagnosing and monitoring various health conditions by assessing the mineral balance in the body.

Alkali metals like sodium and potassium play crucial roles in the human body. Sodium is essential for nerve function, muscle contraction, and fluid balance, while potassium is important for regulating heart rhythm, nerve function, and muscle contractions. Both these alkali metals are needed for proper cellular function and overall health.

No.

Pepsin is an enzyme that breaks down protein to peptides.

Peptidase is another enzyme that breaks down peptides to amino acid.

http://www.answers.com/topic/pepsin

http://www.answers.com/topic/peptidase

Different Enzymes inhibit in different ways. Some are structural analogue of substrate and they compete the substrate in binding to the enzyme. Some inhibitors bind in the active site and prevent the binding of the enzyme. Some enzymes doesn't bind the active site but they change the active site properties that prevent the efficient binding of the substrate. some time substrate in large quantity may inhibit the enzyme, while other times the product formed may do so.

Lactic acid formation is often accompanied by muscle fatigue and soreness during intense or prolonged exercise. It is a byproduct of anaerobic metabolism when the body breaks down glucose for energy production in the absence of sufficient oxygen.

Just the difference between cis and trans isomers. The arrangement of functional groups around double bonded carbons. Same groups lined up on the same side are cis fatties and alternate groups lined up on the different sides are trans fatty acids.

Oil is the world economy's most important source of energy and is, therefore, critical to economic growth. Its value is driven by demand for petroleum products, particularly in the transportation sector. Petroleum products power virtually all motor vehicles, aircraft, marine vessels, and trains around the globe. In total, products derived from oil, such as motor gasoline, jet fuel, diesel fuel, and heating oil, supply nearly 40 percent of the energy consumed by households, businesses, and manufacturers worldwide.

Monosaccharide's consist of only one sugar molecule. (Its the basic molecular unit of all Carbohydrates). Most of them have a carbon backbone that ranges between three to seven carbon atoms. Those carbon atoms also have a hydrogen and a hydroxyl group linked to them.

To make a molecule unsaturated, a double bond would need to be removed. This results in the molecule having fewer hydrogen atoms bonded to the carbon atoms, allowing it to form additional bonds with other atoms or molecules.

Hemoglobin is made up of four "monomeric subunits" each of which is known as a polypeptide and about the size of many normal individual proteins. Each of these subunits has its own tertiary structure and is about the size of another similar globular protein called Myoglobin.

Quarternary structures ONLY exist in proteins with subunits, which are essentially four protein "parts" that are joined together (in this case with Hydrophobic and Ionic interactions) once they are already folded (tertiary structure). 4+ structure is how they fit together.

So Myoglobin, with only one subunit does not have a quarternary structure, but does have primary, secondary and tertiary. Insulin, for example has two subunits and it too will have a quarternary structure, or how both subunits fit together