Alkaline Phosphatase (AP) or basic phosphatase is a homodimeric, membrane-derived glycoprotein of 86 kilodaltons from a bovine intestine. Each monomer of this protein enzyme consist of five cysteine residues, two zinc atoms, and one magnesium atom. The structure contributes to catalytic function of enzyme and optimally active at alkaline pH environments. The abnormal levels of AP in the blood might be associated with the liver, gall bladder or bones issues. Additionally, Kidney tumors, infections and malnutrition have been detected abnormal level of alkaline phosphatase in blood. AP is specific for a broad of molecules including phosphate esters of alcohols, amines, phenols, and pyrophosphates. AP is commonly applied to dephosphorylate proteins and nucleic acids. LPA (Lipoprotein(a)), also known as LP, AK38 or APOA, has a high molecular weight of 501 kDa and located on the chromosome 6q25.3-q26. It is a plasma lipoprotein that is composed of a cholesterol-rich low-density lipoprotein cholesterol (LDL) particle with a molecule of apolipoprotein B100, together with an additional apolipoprotein(a) (Apo(a)), attached by one disulfide bond. LPA codes for the Apo(a) component of the lipoprotein(a) (Lp(a)) particle. This product is a serine proteinase that has capability of autoproteolysis and suppresses the activity of tissue-type plasminogen activator I. The variants of LPA are strongly associated with the high plasma levels of Lp(a) and the increased risk of coronary artery disease (CAD). It is also a risk factor for cardiovascular disease (CVD), stroke, thrombosis and atherosclerosis.