D4159
cis-13,16-Docosadienoic acid
~99% (capillary GC)
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About This Item
Empirical Formula (Hill Notation):
C22H40O2
CAS Number:
Molecular Weight:
336.55
MDL number:
UNSPSC Code:
12352211
PubChem Substance ID:
assay
~99% (capillary GC)
storage temp.
−20°C
SMILES string
CCCCC\C=C\C\C=C\CCCCCCCCCCCC(O)=O
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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G D Schmit et al.
Biophysical journal, 71(6), 3421-3429 (1996-12-01)
It has been suggested that at physiological pH, the trypsin-catalyzed activation of the lipase cofactor, procolipase, to colipase has no consequence for intestinal lipolysis and serves primarily to release the N-terminal pentapeptide, enterostatin, a satiety factor (Larsson, A., and C.
J M Muderhwa et al.
The Journal of biological chemistry, 267(34), 24184-24192 (1992-12-05)
Pancreatic carboxylester lipase catalyzes the exchange of 18O between water and 13,16-cis,cis-doco-sadienoic acid (DA) in monolayers at the argon-buffer interface (Muderhwa, J.M., Schmid, P.C., and Brockman, H.L. (1992) Biochemistry 31, 141). In mixed monolayers of 18O, 18O-DA and 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC)
J M Smaby et al.
Biochemistry, 33(7), 1915-1922 (1994-02-22)
Lipase-catalyzed oxygen exchange between 13,16-cis,cis-docosadienoic acid and water in liquid-expanded monolayers with 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine exhibits abrupt, lipid composition-dependent changes in extent and mechanism [e.g., Muderhwa, J. M. and Brockman, H. L. (1992) J. Biol. Chem. 267, 24184-24192]. The critical nature of
K Aitzetmüller
Lipids, 31(2), 201-205 (1996-02-01)
The current discussion on "renewable resources", and the possibility of gene transfer into rapeseed, has led to many investigations into the biosynthetic pathways leading to industrially useful fatty acids. The various tribes and genera of the plant family Ranunculaceae contain
M Dahim et al.
Biochemistry, 37(23), 8369-8377 (1998-06-19)
Colipase is a cofactor protein which forms a 1:1 complex with pancreatic lipase. This facilitates lipase adsorption to phosphatidylcholine-rich interfaces, presumably as a consequence of the higher affinity of colipase for such interfaces. According to this model, the presence of
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