CHEMISTRY GLOSSARY

pepsin    →   pepsin

Pepsin is the enzyme of gastric juice which razes proteins; it is also used as medicine.

proteases    →   proteaze

Proteases are enzymes which raze proteins during digestion.

protelysis    →   proteoliza

Proteolysis is hydrolytic decomposition of proteins with enzymes, for example trypsin.

cysteine    →   cistein

Cysteine is neutral amino acids with polar side chains. Because of its high reactivity, the thiol group of cysteine has numerous biological functions. It serves as a potent nucleophile and metal ligand (particularly for iron and zinc), but is best known for its ability to form disulfide bonds, which often make an important contribution to the stability of extracellular proteins. Cysteine is a non-essential amino acid, which means that it is biosynthesized in humans.

• Abbreviations: Cys, C
• IUPAC name: 2-amino-3-sulfanylpropanoic acid
• Molecular formula: C₃H₇NO₂S
• Molecular weight: 121.16 g/mol

electrophoresis    →   elektroforeza

Electrophoresis is a technique for the analysis and separation of colloids, based on the movement of charged colloidal particles in an electric field. The migration is toward electrodes of charge opposite to that of the particles. The rate of migration of the particles depends on the field, the charge on the particles, and on other factors, such as the size and shape of the particles.

Electrophoresis is important in the study of proteins. The acidity of the solution can be used to control the direction in which a protein moves upon electrophoresis.

glutamic acid    →   glutaminska kiselina

Glutamic acid is an electrically charged amino acids. It is one of the two amino acids that contain a carboxylic acid group in its side chains. These acids play important roles as general acids in enzyme active centers, as well as in maintaining the solubility and ionic character of proteins. Glutamic acid is commonly referred to as glutamate, because its carboxylic acid side chain will be deprotonated and thus negatively charged in its anionic form at physiological pH. Glutamic acid is referred to as a non-essential amino acid because a healthy human can synthesize all the glutamic acid needed for normal body function from other amino acids.

• Abbreviations: Glu, E
• IUPAC name: 2-aminopentanedioic acid
• Molecular formula: C₅H₉NO₄
• Molecular weight: 147.13 g/mol

glycine    →   glicin

Glycine is the smallest amino acid and is unique because it lacks a side chain. This gives it more conformational freedom than any other amino acid. Glycine is often found in turns and loops where other amino acids would be sterically unacceptable. Although it is formally nonpolar, it’s very small side chain makes no real contribution to hydrophobic interactions. Glycine is not essential to the human diet, as it is biosynthesized in the body from the amino acid serine.

• Abbreviations: Gly, G
• IUPAC name: 2-aminoacetic acid
• Molecular formula: C₂H₅NO₂
• Molecular weight: 75.07 g/mol

isoelectric point    →   izoelektrična točka

Isoelectric point (pI or IEP) is the pH of a solution or dispersion at which the net charge on the molecules or colloidal particles is zero. In electrophoresis there is no motion of the particles in an electric field at the isoelectric point. The net charge (the algebraic sum of all the charged groups present) of any amino acid, peptide or protein, will depend upon the pH of the surrounding aqueous environment. For example, alanine can have a charge of +1, 0, or -1, depending on the pH of the solution in which it is dissolved.

isoleucine    →   izoleucin

Isoleucine is hydrophobic amino acids with aliphatic side chain. It is one of the three amino acids having branched hydrocarbon side chains. The side chains of these amino acids are not reactive but, these residues are critically important for ligand binding to proteins, and play central roles in protein stability. Isoleucine is an essential amino acid, which means that humans cannot synthesize it, so it must be ingested.

• Abbreviations: Ile, I
• IUPAC name: 2-amino-3-methylpentanoic acid
• Molecular formula: C₆H₁₃NO₂
• Molecular weight: 131.12 g/mol

Kjeldahl’s method    →   Kjeldahlov postupak

Kjeldahl’s method is an analytical method for determination of nitrogen in certain organic compounds. The method was developed by the Danish chemist Johan Kjeldahl (1849-1900).

It involves addition of a small amount of anhydrous potassium sulphate to the test compound, followed by heating the mixture with concentrated sulphuric acid, often with a catalyst such as copper sulphate. As a result ammonia is formed. After alkalyzing the mixture with sodium hydroxyde, the ammonia is separated by distillation, collected in standard acid, and the nitrogen determined by back-titration.

1. Kjeldahl flask for decomposition (500 ml – macro or 100 ml - micro)
2. funnel for alkaline solution
3. Wagner tube (drop catcher)
4. condenser
5. absorption flask with known volume of standard acid