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Literature summary extracted from

  • Bensadoun, A.; Ehnholm, C.; Steinberg, D.; Brown, W.V.
    Purification and characterization of lipoprotein lipase from pig adipose tissue (1974), J. Biol. Chem., 249, 2220-2227.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.1.1.34 apolipoprotein-Glu activates Sus scrofa
3.1.1.34 heparin weak stimulation Sus scrofa

General Stability

EC Number General Stability Organism
3.1.1.34 the partially purified enzyme at later stages is stabilized by the inclusion of 20% glycerol in the buffer Sus scrofa

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.1.34 apolipoprotein-Ala
-
 Sus scrofa
3.1.1.34 apolipoprotein-Ser
-
 Sus scrofa

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.1.34 60000
-
 1 * 60000, SDS-PAGE Sus scrofa
3.1.1.34 62000
-
 gel filtration Sus scrofa

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.34 Sus scrofa
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.34
-
 Sus scrofa

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.1.34 adipose tissue
-
 Sus scrofa
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.1.1.34 56.95
-
-
 Sus scrofa

Storage Stability

EC Number Storage Stability Organism
3.1.1.34 -70°C, 1 mg bovine serum albumin per ml or 50% glycerol, stable for several days Sus scrofa

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.34 triolein + H2O
-
 Sus scrofa ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.1.34 monomer 1 * 60000, SDS-PAGE Sus scrofa

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.34 8.8
-
 hydrolysis of triolein Sus scrofa