The effects of raw sweet lupin (Lupinus angustifolius) meal on the growth a
nd N utilisation of rats were determined in two ad libitum and two restrict
ed-feeding net protein utilisation (NPU) and five N balance experiments. Sw
eet lupin seed grown in Western Australia, obtained as meal, either unsuppl
emented (LMU) or fully supplemented with required amino acids (360 g kg(-1)
) (LMFS), was tested. Rats fed lactalbumin (130 g kg(-1)) (LACT) were used
as positive controls, while rats fed a nonprotein diet (NPC) were used as n
egative controls. In addition, seed protein, extracted at pH 7.0 with water
and insoluble after dialysis at pH 7.0 (LPADI; 124 g kg(-1)), was also use
d. The diets contained the same amounts of energy and protein and were supp
lemented with essential amino acids, vitamins and minerals to target requir
ements for rats. Inclusion of LPADI in the diet of growing rats caused urin
ary losses of N, almost all as urea, hypoproteinaemia and increase in body
water that resulted in the lowest NPU values, N balance and growth rate as
compared with other diets used. These rats developed atrophy of the spleen
(low dry weight) and had a comparatively smaller thymus gland than those gi
ven raw meals. Furthermore, the LPADI fraction was shown by sodium dodecyl
sulphate polyacrylamide gel electrophoresis (SDS-PAGE) to contain three pol
ypeptides with molecular weights between 30 and 36kDa which are similar to
lectins obtained from Phaseolus vulgaris, Abrus precatorius and Ricinus com
munis. It is possible that the toxic protein component in the sweet lupin,
which has negligible ie vitro haemagglutination properties and is extremely
toxic ill vivo, exerts toxicity by interfering with protein synthesis in t
he liver, while the immune responses are secondary to azotaemia (high level
of urea in the blood) or cytotoxicity action on lymphocytes. The unusual d
epletion of fat from the body, however, was due to the failure of absorbed
amino acids to assimilate as proteins, creating dietary protein restriction
and leading to lipolysis. It is therefore tentatively suggested that sweet
lupin seed contains a lectin-like protein that is concentrated in this fra
ction. Further purification and biological evaluation to establish the exac
t nature of this protein may be important. (C) 2000 Society of Chemical Ind
ustry.