{'fraction_non_alphanumeric': 0.026334519572953737, 'fraction_numerical': 0.00498220640569395, 'mean_word_length': 5.361990950226244, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Experimental Techniques Used to Decipher Binding Studies of DifferentOrganic Molecules with Serum Albumins

Serum albumins are the most abundant carrier protein in the circulatory system and are involved in the transportation and distribution of exogenous and endogenous materials in blood [1], including nutrients and drugs, mostly by the formation of noncovalent complexes at binding sites [2]. The absorption, distribution, metabolism, and excretion properties as well as the stability and toxicity of drugs can be significantly affected as a result of their binding to serum albumins [3]. Study of the interaction of different types of drugs to serum albumin is extremely important. As a kind of serum albumin, bovine serum albumin (BSA) has the advantages of medical importance, ready availability, low cost, and appreciable ligand/drug-binding properties. Bovine serum albumin (BSA) and human serum albumin (HSA) tertiary structures are also very similar, and the results of all studies are consistent with the fact that they have 76% sequence homology [4]. Several researchers are actively involved in the interaction of several synthesised or ready-made molecules with BSA and HSA to have an understanding of their behaviour. Both spectroscopic techniques and different types of biological assay experiments can be carried out to have a knowledge as to the behaviour of the chemical compounds [5].