Results 211 to 220 of about 529,687 (248)
Differential Release of β-Casomorphins from A1 and A2 Milk During Standardized Gastrointestinal Digestion Quantified by CE-MS. [PDF]
Tehrani T +5 more
europepmc +1 more source
Multigesture Electromyographic Control Complexity in Upper Limb Prostheses Actuated via Single Sensor Input Contraction Magnitude: Qualitative Study for Evaluating Performance and Cognitive Load. [PDF]
Lalle A +12 more
europepmc +1 more source
Some of the next articles are maybe not open access.
Related searches:
Related searches:
Journal of Biochemistry, 2002
Phospholipase A2 (PLA2) catalyzes the hydrolysis of the sn-2 position of membrane glycerophospholipids to liberate arachidonic acid (AA), a precursor of eicosanoids including prostaglandins (PGs) and leukotrienes (LTs). The same reaction also produces lysophosholipids, which represent another class of lipid mediators.
I, Kudo, M, Murakami
openaire +3 more sources
Phospholipase A2 (PLA2) catalyzes the hydrolysis of the sn-2 position of membrane glycerophospholipids to liberate arachidonic acid (AA), a precursor of eicosanoids including prostaglandins (PGs) and leukotrienes (LTs). The same reaction also produces lysophosholipids, which represent another class of lipid mediators.
I, Kudo, M, Murakami
openaire +3 more sources
Seminars in Cell & Developmental Biology, 1997
Mammalian cells contain multiple structurally different phospholipase A2 enzymes that hydrolyse sn-2 fatty acid from membrane phospholipid. The low molecular weight secreted forms act extracellularly both as lipolytic enzymes and as agonists that bind to specific cell surface receptors.
, Gijón, , Leslie
openaire +2 more sources
Mammalian cells contain multiple structurally different phospholipase A2 enzymes that hydrolyse sn-2 fatty acid from membrane phospholipid. The low molecular weight secreted forms act extracellularly both as lipolytic enzymes and as agonists that bind to specific cell surface receptors.
, Gijón, , Leslie
openaire +2 more sources
2015
Lipofuscin is highly fluorescent material, formed in several tissues but best studied in the eye. The accumulation of lipofuscin in the retinal pigment epithelium (RPE) is a hallmark of aging in the eye and has been implicated in various retinal degenerations, including age-related macular degeneration.
Rosalie K, Crouch +4 more
openaire +2 more sources
Lipofuscin is highly fluorescent material, formed in several tissues but best studied in the eye. The accumulation of lipofuscin in the retinal pigment epithelium (RPE) is a hallmark of aging in the eye and has been implicated in various retinal degenerations, including age-related macular degeneration.
Rosalie K, Crouch +4 more
openaire +2 more sources
Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 2004
Phospholipase A2 (PLA2) is an enzyme present in snake and other venoms and body fluids. We measured PLA2 catalytic activity in tissue homogenates of 22 species representing the classes Anthozoa, Hydrozoa, Scyphozoa and Cubozoa of the phylum Cnidaria. High PLA2 levels were found in the hydrozoan fire coral Millepora sp.
Nevalainen, Timo J. +6 more
openaire +3 more sources
Phospholipase A2 (PLA2) is an enzyme present in snake and other venoms and body fluids. We measured PLA2 catalytic activity in tissue homogenates of 22 species representing the classes Anthozoa, Hydrozoa, Scyphozoa and Cubozoa of the phylum Cnidaria. High PLA2 levels were found in the hydrozoan fire coral Millepora sp.
Nevalainen, Timo J. +6 more
openaire +3 more sources
Nature, 1961
THE heterogeneity of adult human haemoglobin is a well-established fact1–3. The present work was designed to determine if the slow electrophoretic fraction A2 has antigenic specificity and if this fraction can be detected immunologically in cord blood and in the presence of haemoglobin S and C.
P, HELLER, V, YAKULIS, A M, JOSEPHSON
openaire +2 more sources
THE heterogeneity of adult human haemoglobin is a well-established fact1–3. The present work was designed to determine if the slow electrophoretic fraction A2 has antigenic specificity and if this fraction can be detected immunologically in cord blood and in the presence of haemoglobin S and C.
P, HELLER, V, YAKULIS, A M, JOSEPHSON
openaire +2 more sources
Prostaglandins & Other Lipid Mediators, 2002
Phospholipase A2 (PLA2) catalyzes the hydrolysis of the sn-2 position of membrane glycerophospholipids to liberate arachidonic acid (AA), a precursor of eicosanoids including prostaglandins and leukotrienes. The same reaction also produces lysophosholipids, which represent another class of lipid mediators.
Ichiro, Kudo, Makoto, Murakami
openaire +2 more sources
Phospholipase A2 (PLA2) catalyzes the hydrolysis of the sn-2 position of membrane glycerophospholipids to liberate arachidonic acid (AA), a precursor of eicosanoids including prostaglandins and leukotrienes. The same reaction also produces lysophosholipids, which represent another class of lipid mediators.
Ichiro, Kudo, Makoto, Murakami
openaire +2 more sources
Haemoglobin A2 (Hb A2) and malaria.
The Central African journal of medicine, 1994The Packed Cell Volume (PCV), reticulocyte count and Hb A2 were determined in 28 patients during the period of malaria parasitaemia and 14 days after effective treatment. The Hb A2 was determined by cellulose acetate haemoglobin electrophoresis in alkaline medium followed by elution in water.
P O, Olatunji +3 more
openaire +1 more source
Nature, 1960
AT least two forms of adult haemoglobin are present in the blood of the normal human adult, a main component haemoglobin A1 and a minor one haemoglobin A2 (ref. 1). In normal individuals the concentration of haemoglobin A2 is about 2.5 per cent of the total haemoglobin. In persons heterozygous for the Cooley gene, this amount is increased to a level of
C J, MULLER, J H, JONXIS
openaire +2 more sources
AT least two forms of adult haemoglobin are present in the blood of the normal human adult, a main component haemoglobin A1 and a minor one haemoglobin A2 (ref. 1). In normal individuals the concentration of haemoglobin A2 is about 2.5 per cent of the total haemoglobin. In persons heterozygous for the Cooley gene, this amount is increased to a level of
C J, MULLER, J H, JONXIS
openaire +2 more sources

