scholarly journals The penetration of serum albumin into phospholipid monolayers of different fatty acid chain length and interfacial charge

1970 ◽  
Vol 119 (1) ◽  
pp. 21-25 ◽  
Author(s):  
P. Quinn ◽  
R. M. C. Dawson
Keyword(s):  
Fatty Acid ◽  
Phosphatidic Acid ◽  
Serum Albumin ◽  
Water Interface ◽  
Fatty Acid Chain ◽  
Phospholipid Monolayers ◽  
Oppositely Charged ◽  
Interfacial Charge ◽  
Positively Charged ◽  
Long Chain

1. The highest surface pressure of phosphatidylcholine monolayers allowing penetration of delipidated serum albumin decreased in the order dibehenoyl>distearoyl>dipalmitoyl=dimyristoyl. This pressure was not related to the area occupied or to the space available between the phospholipid molecules at the interface. 2. Penetration of albumin into yeast phosphatidylcholine monolayers was increased by adding a small percentage of long-chain anions (phosphatidic acid, dicetylphosphoric acid) to the film but only when the protein was below its isoelectric point (i.e. positively charged). 3. Stearylamine added to phosphatidylcholine monolayers had no effect on albumin penetration even when the protein was oppositely charged to that of the phospholipid/water interface. 4. The results are discussed in relation to the activation of certain phospholipases by anionic amphipathic substances.

Triglyceride Fatty Acid Chain Length Influences the Post Prandial Rise in Serum Intestinal Alkaline Phosphatase Activity

1992 ◽  
Vol 29 (3) ◽  
pp. 287-291 ◽  
Author(s):  
A P Day ◽  
M D Feher ◽  
R Chopra ◽  
P D Mayne
Keyword(s):  
Fatty Acid ◽  
Chain Length ◽  
Chain Fatty Acid ◽  
Intestinal Alkaline Phosphatase ◽  
Long Chain Fatty Acid ◽  
Fatty Acid Chain Length ◽  
Healthy Humans ◽  
Fatty Acid Chain ◽  
Long Chain ◽  
Fatty Acid Triglycerides

Intestinal alkaline phosphatase (IALP) activity rises following the ingestion of a fat-containing meal. Previous studies on intestinal fluid and lymph have shown that the magnitude of this response is dependent upon fatty acid chain length. To examine this relation in the serum of healthy humans, 10 subjects consumed two standardized fat meals. One meal contained predominantly long chain fatty acid triglycerides, the other contained predominantly medium chain fatty acid triglycerides. Serum IALP activity was measured in serial blood samples using a sensitive immunological assay. IALP activity was ABO blood group and secretor status dependent. The post-prandial rise in serum IALP activity was significantly greater following the long chain fatty acid meal than following the medium chain fatty acid meal. Previous observations of the fatty acid chain length dependency of the IALP response to fat ingestion, therefore, also apply in the serum of healthy humans under normal physiological conditions. Standardized fat meals provide the basis of a useful method for the investigation of the role of IALP in fat absorption.

Binding of some long-chain fatty acid anions and alcohols by bovine serum albumin

Biochemistry ◽  
1968 ◽  
Vol 7 (4) ◽  
pp. 1357-1361 ◽  
Author(s):  
Jacqueline A. Reynolds ◽  
Sarah. Herbert ◽  
Jacinto. Steinhardt
Keyword(s):  
Fatty Acid ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Chain Fatty Acid ◽  
Long Chain Fatty Acid ◽  
Long Chain

scholarly journals The synthesis and hydrolysis of long-chain fatty acyl-coenzyme A thioesters by soluble and microsomal fractions from the brain of the developing rat

1976 ◽  
Vol 160 (2) ◽  
pp. 247-251 ◽  
Author(s):  
P J Brophy ◽  
D E Vance
Keyword(s):  
Fatty Acid ◽  
Microsomal Fraction ◽  
Specific Activity ◽  
Arachidic Acid ◽  
Fatty Acyl ◽  
Chain Elongation ◽  
Fatty Acid Chain ◽  
Specific Activities ◽  
Coa Hydrolase ◽  
Long Chain

1. The specific activities of long-chain fatty acid-CoA ligase (EC6.2.1.3) and of long-chain fatty acyl-CoA hydrolase (EC3.1.2.2) were measured in soluble and microsomal fractions from rat brain. 2. In the presence of either palmitic acid or stearic acid, the specific activity of the ligase increased during development; the specific activity of this enzyme with arachidic acid or behenic acid was considerably lower. 3. The specific activities of palmitoyl-CoA hydrolase and of stearoyl-CoA hydrolase in the microsomal fraction decreased markedly (75%) between 6 and 20 days after birth; by contrast, the corresponding specific activities in the soluble fraction showed no decline. 4. Stearoyl-CoA hydrolase in the microsomal fraction is inhibited (99%) by bovine serum albumin; this is in contrast with the microsomal fatty acid-chain-elongation system, which is stimulated 3.9-fold by albumin. Inhibition of stearoyl-CoA hydrolase does not stimulate stearoyl-CoA chain elongation. Therefore it does not appear likely that the decline in the specific activity of hydrolase during myelogenesis is responsible for the increased rate of fatty acid chain elongation. 5. It is suggested that the decline in specific activity of the microsomal hydrolase and to a lesser extent the increase in the specific activity of the ligase is directly related to the increased demand for long-chain acyl-CoA esters during myelogenesis as substrates in the biosynthesis of myelin lipids.

scholarly journals Mechanism of Long-Chain Free Fatty Acid Protonation at the Membrane-Water Interface

2018 ◽  
Vol 114 (9) ◽  
pp. 2142-2151 ◽  
Author(s):  
Alina A. Pashkovskaya ◽  
Mario Vazdar ◽  
Lars Zimmermann ◽  
Olga Jovanovic ◽  
Peter Pohl ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Free Fatty Acid ◽  
Water Interface ◽  
Long Chain
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