scholarly journals Differential growth requirements of serum factors (bovine serum albumin and low density lipoprotein) for normal and transformed human cells in a serum-free culture.

1983 ◽  
Vol 8 (1) ◽  
pp. 67-75 ◽  
Author(s):  
Hiroyoshi Hoshi ◽  
Mikio Kan ◽  
Isao Yamane ◽  
Tadao Ohno ◽  
Masayoshi Namba
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Low Density ◽  
Differential Growth ◽  
Serum Factors ◽  
Serum Free ◽  
Growth Requirements

scholarly journals Binding characteristics of reduced hepatic receptors for acetylated low-density lipoprotein and maleylated bovine serum albumin

1990 ◽  
Vol 265 (3) ◽  
pp. 689-698 ◽  
Author(s):  
E Ottnad ◽  
D P Via ◽  
H Sinn ◽  
E Friedrich ◽  
R Ziegler ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Binding Sites ◽  
Bovine Serum ◽  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Low Density ◽  
Binding Characteristics ◽  
Bsa Binding ◽  
35 Kda Protein

The binding characteristics of reduced hepatic membrane proteins for acetylated low-density lipoprotein (acetyl-LDL) and maleylated bovine serum albumin (Mal-BSA) have been examined. Two receptor activities were extracted from hepatic membranes in the presence of octyl beta-D-glucoside and beta-mercaptoethanol, and were separated by chromatography on Mal-BSA-Sepharose 4B. The receptors were revealed by ligand blotting. The active binding proteins had apparent molecular masses of 35 and 15 kDa in SDS/polyacrylamide gels. Equilibrium studies with protein-phosphatidylcholine complexes indicated that the reduced 35 kDa protein expresses two binding sites for Mal-BSA and one for acetyl-LDL, whereas the 15 kDa protein-phosphatidylcholine complex binds 131I-Mal-BSA and 131I-acetyl-LDL with a 4:1 stoichiometry. 131I-Mal-BSA binding was linear with both proteins, with a Kd of 4.8 nM at the 35 kDa protein and a Kd of 5.6 nM at the 15 kDa protein. The 35 kDa protein displayed saturable binding of 131I-acetyl-LDL with a Kd of 5 nM; the 15 kDa binding protein bound 131I-acetyl-LDL with a Kd of 2.3 nM. A 85 kDa protein was obtained by Mal-BSA-Sepharose chromatography when the hepatic membranes had been solubilized with Triton X-100 in presence of GSH/GSSG. This protein displayed saturable 131I-Mal-BSA binding with a Kd of 30 nM and 131I-acetyl-LDL binding with a Kd of 6.5 nM. The 131I-Mal-BSA binding capacity was four times higher than that of 131I-acetyl-LDL. Competition studies with the 35 kDa, 15 kDa and 85 kDa proteins binding Mal-BSA, acetyl-LDL, formylated albumin and polyanionic competitors provide evidence for the existence of more than one class of binding sites at the reduced binding proteins.

scholarly journals Evidence in liver for a disulphide-linked scavenger receptor containing a binding site for acetylated low-density lipoprotein and maleylated bovine serum albumin

1988 ◽  
Vol 253 (3) ◽  
pp. 835-838 ◽  
Author(s):  
E Ottnad ◽  
D P Via ◽  
H Sinn ◽  
E Friedrich ◽  
R Ziegler ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Binding Site ◽  
Bovine Serum ◽  
Low Density Lipoprotein ◽  
Scavenger Receptor ◽  
Density Lipoprotein ◽  
Low Density ◽  
Bsa Binding ◽  
35 Kda Protein

Membranes from rat liver were analysed under reducing conditions. The components of the soluble membranes responsible for the binding of acetylated low density lipoprotein (acetyl-LDL) and maleylated bovine serum albumin (Mal-BSA) were chromatographed on a polyethyleneimine-cellulose column and subsequently separated by gel electrophoresis. For both ligands a major binding protein (Mr = 35,000) was revealed by ligand blotting. A minor protein (Mr greater than 67,000) exhibited little binding. The Scatchard plot of the 131I-Mal-BSA binding data of the 35 kDa protein was linear, with a Kd of 17.3 nM. High concentrations of acetyl-LDL competed for half of the 131I-Mal-BSA binding. Excessive Mal-BSA competed for all the visible acetyl-LDL binding. The findings indicate the existence, in the reduced hepatic membrane, of a 35 kDa protein that has two binding sites for 131I-Mal-BSA and one binding site for acetyl-LDL.

Purified low-density lipoprotein and bovine serum albumin efficiency to internalise lycopene into adipocytes

2008 ◽  
Vol 46 (12) ◽  
pp. 3832-3836 ◽  
Author(s):  
Erwan Gouranton ◽  
Claire El Yazidi ◽  
Nicolas Cardinault ◽  
Marie Josèphe Amiot ◽  
Patrick Borel ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Low Density

scholarly journals Binding of acetylated low density lipoprotein and maleylated bovine serum albumin to the rat liver: one or two receptors?

1987 ◽  
Vol 6 (2) ◽  
pp. 319-326 ◽  
Author(s):  
H.A. Dresel ◽  
E. Friedrich ◽  
D.P. Via ◽  
H. Sinn ◽  
R. Ziegler ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Rat Liver ◽  
Bovine Serum ◽  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Low Density

Rat carcinoma cells in long-term, serum-free culture provide a continuing supply of collagenase

1985 ◽  
Vol 5 (12) ◽  
pp. 1071-1077 ◽  
Author(s):  
Geoffrey A. Stevenson ◽  
J. Guy Lyons ◽  
David A. Cameron ◽  
Robert L. O'Grady
Keyword(s):  
Epithelial Cells ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Mammary Carcinoma ◽  
Bovine Serum ◽  
Defined Medium ◽  
Carcinoma Cells ◽  
Serum Free ◽  
Vertebrate Collagenase

Neoplastic, epithelial cells derived from a spontaneously-arising rat mammary carcinoma have been cultured in a defined medium, in the absence of serum, continuously, for over 2 years. The medium is a mixture of Ham's F12 and Dulbecco's Modified Eagle's media supplemented with insulin, transferrin and bovine serum albumin. The cells have retained their potential to produce tumours and, in culture, a true vertebrate collagenase. This system provides a continuing supply of vertebrate collagenase through the application of recently developed methods.

Selective aggregation of zinc phthalocyanines in the skin

2000 ◽  
Vol 04 (03) ◽  
pp. 278-284 ◽  
Author(s):  
KENJI TABATA ◽  
KAORU FUKUSHIMA ◽  
KAZUO ODA ◽  
ICHIRO OKURA
Keyword(s):  
Photodynamic Therapy ◽  
Side Effects ◽  
Bovine Serum Albumin ◽  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
The Other ◽  
Low Density ◽  
Monomeric Form ◽  
Zinc Phthalocyanines ◽  
Selective Aggregation

In photodynamic therapy it is important to avoid undesirable side effects caused by photodynamic reactions with accumulated photosensitizers, especially in the skin. Although phthalocyanine monomers can serve as photosensitizers, aggregated phthalocyanines are inactive. In this study the aggregations of five zinc phthalocyanines (MSPc, TSPc, TX-101A, TX-105A and TX-106A) in the skin and in the tumor are compared. Every phthalocyanine was more dissociated in the tumor than in the skin. In particular, TX-101A and TX-106A remained in monomeric form in the tumor but were aggregated in the skin. The aggregation effects of phthalocyanines in organic solvents and biological materials were also investigated. These phthalocyanines were aggregated in water and ethanol and also by the addition of bovine serum albumin and ghosts of red cells. On the other hand, they were dissociated in propanol and also by the addition of low-density lipoprotein. It was found that the dissociation of these phthalocyanines depended strongly on the polarity of the solvents and on the biological microenvironment.

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