Topic
Bovine serum albumin
About: Bovine serum albumin is a research topic. Over the lifetime, 19981 publications have been published within this topic receiving 571291 citations. The topic is also known as: BSA.
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TL;DR: The chaperone-like activity of serum albumin suggests it protects against protein misfolding and aggregation, and may have implications for protein mis Folding disorders of the extracellular compartment.
129 citations
TL;DR: It is found that BSA and LYZ can be readily immobilized on SAMs at their isoelectric point (IEP), and the strong hydrophobic interaction at the IEP is attributed to immobilization.
Abstract: The immobilization of protein molecules on self-assembled monolayers (SAM) by physical interactions and chemical bonding has been studied using atomic force microscopy (AFM). The proteins used for our investigation are bovine serum albumin (BSA), lysozyme (LYZ), and normal rabbit immunoglobulin G (IgG). The surfaces are methyl-, hydroxyl-, carboxylic acid- and aldehyde-terminated SAMs. We found that BSA and LYZ can be readily immobilized on SAMs at their isoelectric point (IEP). The detailed surface morphology of adsorbed proteins varies with the functionality of the SAMs. The strong hydrophobic interaction at the IEP is attributed to immobilization. If the solution pH is deviated from the IEP, proteins may be attached onto the surface via electrostatic interactions. Covalent binding between the aldehyde-terminated SAM and the H2N-groups in the protein results in immobilization of all three proteins. The individual proteins and their orientations on SAMs are clearly resolved from high-resolution AFM images. The stability and bioactivity of these immobilized proteins are also studied.
129 citations
TL;DR: Synthetic peptides derived from human fibrin were unidirectionally conjugated to three carrier proteins by a method that employs N-succinimidyl bromoacetate, a heterobifunctional crosslinking reagent prepared with a 79% yield in gram quantities from inexpensive starting materials.
128 citations
TL;DR: Polyvinylalcohol was tested as a replacement for protein in supporting motility, acrosome reactions, and fertilizing ability of hamster spermatozoa in vitro and it was suggested that PVA may find general application in cell culture media.
Abstract: Polyvinylalcohol (PVA) was tested as a replacement for protein (bovine serum albumin, BSA) in supporting motility, acrosome reactions, and fertilizing ability of hamster spermatozoa in vitro. Bovine serum albumin is normally required for all of these processes. After incubation for 5--6 hours in a simple culture medium containing BSA and PVA (0.1 mg/ml) and essential low molecular weight factors from blood serum, 85% of motile spermatozoa had undergone acrosome reactions. Sperm motility was equally well maintained by PVA in the absence of BSA but virtually no spermatozoa showed acrosome reactions even after prolonged incubation. Serum factors were later replaced by hypotaurine (10 microM), isoproterenol (1 microM), and penicillamine (20 microM). Spermatozoa incubated in this defined medium with BSA alone or with BSA and PVA fertilized more than 90% of oocytes. No oocytes were penetrated when BSA was replaced by PVA although vigorous sperm motility was maintained. Polyvinylalcohol may help elucidate the mechanism of the acrosome reaction by permitting effects of protein and other substances to be studied without loss of sperm motility (viability). Polyvinylalcohol could also replace BSA in solutions used for manipulation of zona pellucida-free oocytes. It is suggested that PVA may find general application in cell culture media.
128 citations
TL;DR: It is shown that E. coli extracts degraded casein and globin polypeptides at rapid rates but showed little activity with native proteins such as superoxide dismutase, hemoglobin, bovine serum albumin, or catalase when these same proteins were denatured by exposure to oxygen radicals or H2O2, however, they became excellent substrates for degradation in E. bacteria extracts.
128 citations