Catabolism - breaking down of large molecules into smaller ones
Ammonia (NH3)
Comes from the decomposition of proteins and the conversion of amino acids in cellular respiration to ATP molecules
Carbohydrates
Organic molecules containing carbon, hydrogen, and oxygen in a ratio near 1:2:1
Carbohydrates
Ribose and deoxyribose (parts of RNA and DNA)
Sugars, starch, glycogen (energy storage)
Cellulose and chitin (cell strengthening)
Lipids
Insoluble in water, include fats, phospholipids, steroids, prostaglandins
Proteins
Composed of carbon, hydrogen, oxygen, and nitrogen covalently bonded
Functions of proteins
Part of cell membranous structures
Enzymes
Antibodies
Source of energy converted to ATP
Nucleic acids
DNA and RNA, composed of CHONP
Adenosine triphosphate (ATP)
Energy stored in the ATP molecule is used to run the cell and perform activities such as repair, reproduction, assimilation, and transport of materials across cell membranes
pH
Defined as the negative logarithm of the hydrogen ion concentration in moles/liter
Acidosis
Abnormal physiological state caused by low blood pH (below 7.35)
Alkalosis
Abnormal physiological state caused by high blood pH (above 7.45)
Blood pH above 7.8 generally causes uncontrollable and sustained skeletal muscle contractions
Buffers
Compounds that stabilize the pH of a solution by removing or replacing H+
Buffer systems
Usually involve a weak acid and its related salt, which functions as a weak base
Buffers and buffer systems in body fluids help maintain the pH within normal limits
Organic compounds
Made up of long chains of carbon atoms linked by covalent bonds, forming additional covalent bonds with H+, O2, N2, P, S, Fe, or other elements
Macromolecules
Include carbohydrates, lipids, proteins, and nucleic acids
Monomers
Subunits that are bonded to other identical molecules to form a polymer
Dehydration synthesis
Reaction where monomers are joined together to form a polymer
Hydrolysis
Reaction where polymers are separated or released into their monomer subunits
Glucose
A monosaccharide carbohydrate
Glycogen (animal starch) does not dissolve in water or other body fluids
Lipids make up 12–18% of the total body weight of adult men, and 18–24% for adult women
Most lipids are hydrophobic, or insoluble in water, but special transport mechanisms carry them into the bloodstream
Classes of lipids
Fatty acids
Eicosanoids
Glycerides
Steroids
Phospholipids and glycolipids
Saturated fatty acids
Contain only single covalent bonds, found in whole milk, butter, eggs, beef, pork, and coconut and palm oils
Eicosanoids
Lipids derived from arachidonic acid, a fatty acid that must be absorbed in the diet because the body cannot synthesize it; include leukotrienes and prostaglandins
Prostaglandins
Compounds released by cells to coordinate or direct local cellular activities, extremely powerful even in small quantities
Glycerides
Include triglycerides (triacylglycerols or neutral fat), an energy source, insulation, and protection
Steroids
Differ in the functional groups attached to the basic framework, include cholesterol and steroid hormones
Lipid reserves retain both valuable lipid-soluble vitamins (A, D, E, K) and potentially dangerous lipid-soluble pesticides
Prostaglandins
Compounds released by cells to coordinate or direct local cellular activities, and they are extremely powerful even in small quantities. Also known as local hormones
Glycerides
Triglycerides, also known as triacylglycerols or neutral fat; energy source, insulation, protection
Cholesterol
Contained in plasma membrane
Functions of proteins
Support (structural proteins)
Movement (contractive proteins)
Transport (transport proteins)
Buffering
Metabolic regulation (enzymes)
Coordination and control (protein hormones)
Defense (special clotting proteins)
Protein shape
Determines its functional characteristics, and the sequence of amino acids ultimately determines its shape
Primary structure of a protein
Determined by its amino acid sequence
Secondary structure of a protein
Determined by the hydrogen bonds between amino acids that cause the protein to coil into helices or pleated sheets. This shape is crucial to the functioning of proteins. Once H-bonds are destroyed proteins becomes nonfunctional
Tertiary structure of a protein
A secondary folding caused by interactions within the peptide bonds and between sulfur atoms of different amino acids