Biomaterial Database

Interaction of alpha-lactalbumin with phospholipid vesicles as studied by photoactivated hydrophobic labeling. 1989

J Kim, and H Kim

Department of Biological Science and Engineering, Korea Advanced Institute of Science, Seoul.

The alpha-lactalbumin segment which penetrates into phosphatidylserine/phosphatidylethanolamine vesicle bilayer under acidic condition was photoactively labeled with 3-(trifluoromethyl)-3-(m-[125I]iodophenyl)diazirine [( 125I]TID) which had been partitioned into the hydrophobic interior of the bilayer. The hydrophobically labeled amino acid residues were identified by trypsin digestion of the alpha-lactalbumin/vesicle complex, extraction and Edman degradation of the membrane embedded fragment. The results are consistent with a notion that the segment exists in the membrane as an alpha-helix and that only one surface of this alpha-helix is exposed to the hydrophobic interior of the bilayer. Possible models are: (a) a loop of tightly held alpha-helix penetrating deep into the bilayer and (b) the helix being located on the interface between bilayer and the aqueous solution. The time-dependent [125I]TID labeling process revealed that the middle part of this segment goes into the bilayer first and is then followed by both ends. The penetration rate is comparable to that of the fusion of the lipid vesicles of the same composition by alpha-lactalbumin at the same pH, which further supports that the penetration is the cause of fusion.

UI	MeSH Term	Description	Entries
D007457	Iodine Radioisotopes	Unstable isotopes of iodine that decay or disintegrate emitting radiation. I atoms with atomic weights 117-139, except I 127, are radioactive iodine isotopes.	Radioisotopes, Iodine
D007768	Lactalbumin	A major protein fraction of milk obtained from the WHEY.	alpha-Lactalbumin,alpha-Lactalbumin A,alpha-Lactalbumin B,alpha-Lactalbumin C,alpha Lactalbumin,alpha Lactalbumin A,alpha Lactalbumin B,alpha Lactalbumin C
D008051	Lipid Bilayers	Layers of lipid molecules which are two molecules thick. Bilayer systems are frequently studied as models of biological membranes.	Bilayers, Lipid,Bilayer, Lipid,Lipid Bilayer
D008962	Models, Theoretical	Theoretical representations that simulate the behavior or activity of systems, processes, or phenomena. They include the use of mathematical equations, computers, and other electronic equipment.	Experimental Model,Experimental Models,Mathematical Model,Model, Experimental,Models (Theoretical),Models, Experimental,Models, Theoretic,Theoretical Study,Mathematical Models,Model (Theoretical),Model, Mathematical,Model, Theoretical,Models, Mathematical,Studies, Theoretical,Study, Theoretical,Theoretical Model,Theoretical Models,Theoretical Studies
D008969	Molecular Sequence Data	Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.	Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D010446	Peptide Fragments	Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.	Peptide Fragment,Fragment, Peptide,Fragments, Peptide
D010714	Phosphatidylethanolamines	Derivatives of phosphatidic acids in which the phosphoric acid is bound in ester linkage to an ethanolamine moiety. Complete hydrolysis yields 1 mole of glycerol, phosphoric acid and ethanolamine and 2 moles of fatty acids.	Cephalin,Cephalins,Ethanolamine Phosphoglyceride,Ethanolamine Phosphoglycerides,Ethanolamineglycerophospholipids,Phosphoglyceride, Ethanolamine,Phosphoglycerides, Ethanolamine
D010718	Phosphatidylserines	Derivatives of PHOSPHATIDIC ACIDS in which the phosphoric acid is bound in ester linkage to a SERINE moiety.	Serine Phosphoglycerides,Phosphatidyl Serine,Phosphatidyl Serines,Phosphatidylserine,Phosphoglycerides, Serine,Serine, Phosphatidyl,Serines, Phosphatidyl
D011487	Protein Conformation	The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).	Conformation, Protein,Conformations, Protein,Protein Conformations
D000595	Amino Acid Sequence	The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.	Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein