Characterization of rat adipose tissue lipoprotein lipase using a monospecific antibody

Vydelingum, N.; Al-Quadan, Farouk; Kissebah, Ahmed H.; Etienne, J

doi:10.1016/0005-2760(86)90026-3

Cited by 7 publications

(2 citation statements)

References 40 publications

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“…It is most likely that the additional bands were representative of LPL degradation products (Socorro and Jackson, 1985) and/or incompletely processed forms of the enzyme (Amri et al, 1986). Vydelingum et al (1986) noted, however, that only one major species of the LPL revealed on immunoblots was glycosylated, and in the present case no such secondary bands were noted when enzyme isolated from each tissue was investigated.…”

Section: Discussioncontrasting

confidence: 49%

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Distinct immunoreactivities suggest the existence of potential tissue variants in rat lipoprotein lipase

Soteriou

Cryer

1994

Biochemical Journal

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Lipoprotein lipases (LPL) isolated from rat cardiac muscle and bovine milk were each used as immunogens to produce polyclonal anti-LPL sera and two anti-LPL monoclonal antibodies. The immunological reactivities of these antibody sources with LPL purified from rat cardiac muscle, lung, adipose tissue, mammary gland and skeletal muscle were compared by an e.l.i.s.a. and by Western blotting. Differences between the immunoreactivities of LPL from the distinct tissue sources were revealed in both systems. A synthetic peptide with a sequence corresponding to the heparin-binding site of LPL (Ser-Arg-Thr-Asn-Thr-Lys-Val-Ser-Arg-Ile-Thr-Gly-Leu) was produced and used as an immunogen. The antiserum produced against the synthetic peptide was found to bind specifically to the region of the heparin-binding site, as determined by use of a competition e.l.i.s.a. In use against the five tissue LPL preparations, this antiserum revealed only minor variations between the tissue sources, compared with the hierarchy of reactivity observed when antibodies raised against the whole molecule were used. In combination with the outcome of previous studies on some of the physical properties of these preparations [Soteriou and Cryer (1993) Int. J. Biochem. 25, 1483-1490], the observations reported here on the distinct immunoreactivities exhibited by LPL prepared from the different tissue sources of a single species indicate the necessity to characterize fully the nature of these differences.

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Section: Discussioncontrasting

confidence: 49%

“…The use ofantibodies as tools in the investigation of the properties of individual LPL preparations has been described previously (e.g. Vydelingum et al, 1986;Friedman et al, 1986). However, the present study compares the immunological characteristics of isolated LPL from five different tissue sources taken from a single species.…”

Section: Discussionmentioning

confidence: 98%