Lupinal

M.p. 234-235 C. Hydrolyses to aspartic acid. L-asparagine can be prepared from lupin seedlings, and DL-asparagine is synthesised from ammonia and maleic anhydride. L-asparagine is very widely distributed in plants, being found in all the Leguminosae and Gramineae, and in many other seeds, roots and buds. 

Lunar caustic Lundin process Lung cancer Lung edema Lung flukes Lungworms a-Lupilic acid b-Lupilic acid Lupin... 

Feeding experiments utilizing C-, N-, and H-labeled cadaverine (44) and lysine (24) in l upinus augustifolius a source of the lupine alkaloids (—)-sparteine (50, R = H,H) and (+)-lupanine (50, R = O), have been reported which lend dramatic credence to the entire biosynthetic sequence for these and the related compounds discussed above (41). That is, the derivation of these bases is in concert with the expected cyclization from the favored aH-trans stereoisomer of the trimer expected on self-condensation of the 1-dehydropiperidine (45). 

Raw soybeans also maybe used as a supplemental protein source. Dry beans, ie, beans normally harvested in the green / imm a tiire state, fava beans, lupins, field peas, lentils, and other grain legumes are potential supplemental protein sources however, several of these may have deleterious effects, predominantly enzyme inhibition, on the animal. The supply of each is limited (5). 

LPC Product Quality. Table 10 gives approximate analyses of several LPC products. Amino acid analyses of LPC products have been pubhshed including those from alfalfa, wheat leaf, barley, and lupin (101) soybean, sugar beet, and tobacco (102) Pro-Xan LPC products (100,103) and for a variety of other crop plants (104,105). The composition of LPCs varies widely depending on the raw materials and processes used. Amino acid profiles are generally satisfactory except for low sulfur amino acid contents, ie, cystine and methionine. 

Vegetable proteins other than that from soy have potential appHcability in food products. Functional characteristics of vegetable protein products are important factors in determining their uses in food products. Concentrates or isolates of proteins from cotton (qv) seed (116), peanuts (117), rape seed (canola) (118,119), sunflower (120), safflower (121), oats (122), lupin (123), okra (124), and com germ (125,126) have been evaluated for functional characteristics, and for utility in protein components of baked products (127), meat products (128), and milk-type beverages (129) (see Dairy substitutes). 

Lupine seed, though used primarily in animal feeds (see Feeds AND FEED ADDITIVES), does have potential for use in human appHcations as a replacement for soy flour, and is reported to contain both trypsin inhibitors and hemagglutenins (17). The former are heat labile at 90°C for 8 minutes the latter seem much more stable to normal cooking temperatures. Various tropical root crops, including yam, cassava, and taro, are also known to contain both trypsin and chymotrypsin inhibitors, and certain varieties of sweet potatoes may also be impHcated (18). 

A Phenylthalamic Acid. A product of Hungary, A/-phenylthalamic acid [4727-29-1] (Nevirol) (43), is a ben2oic acid derivative not sold in the United States. It is used to increase pollination and results in setting more fmit when weather conditions are unfavorable for normal ferti1i2ation. It is employed in both greenhouses and fields on apples, beans, cherries, lupine, peas, peppers, soybeans, and sunflower (23). 

It has become customary to call the principal members of this group the lupin alkaloids, but in view of their wide distribution in the Papilionaceae, a better title is that suggested above, since they appear to be the characteristic alkaloids of this leguminous sub-family. This is not the only type of alkaloid found in the Leguminosae other types occur, e.g., in Acacia (p. 631), Crotalaria (p. 601), Erythrina (p. 386), Mimosa (p. 4) and Pentaclethra (p. 776). 

Smirnova and Moshkov have investigated the effects of the removal of leaves or buds and of grafting on the alkaloidal content of lupins, and Wallebroek has studied the alkaloidal and nitrogenous metabolism of Lupinus luteus seeds on germination. ... 

Owing to the use of lupin seeds for feeding animals, much attention has been given to the selection of species free from the more toxic alkaloids of the group, particularly sparteine, to methods of removing alkaloids from the seeds, a subjeet on which there is an extensive literature and to methods of estimating alkaloids in lupins on which a critical review has been published by Brahm and Andresen. ... 

Sparteine (43) is oxidized to a mixture of isomers /J -didehydro-sparteine (44) and id -dehydrosparteine (45) (57). The other two stereoisomers of sparteine, a-isosparteine (46) (3S,j9) and S-isosparteine (sparta-lupine) (47) (58,60) have been subjected to mercuric acetate oxidation, each giving Zl -didehydrosparteine (44). 

Rothwell and Wain (126) have isolated in crystalline form a growth inhibitor from Lupinus luteus (yellow lupine) pods which they have partially characterized. Analytical data suggested that the inhibitor possessed the characteristics of an unsaturated hydroxyketo acid. Inhibition in the wheat coleoptile cylinder test was obtained with concentrations of 0.25 to 1.0 p.p.m. 

Garlic, sweet potato, wheat, barley, sunflower, bean (mung), sesame, lupine, strawberry, artichke (Jerusalem), bean (kidney), bean (lima), groundnut/peanut Moderately sensitive (1.0-2.0ppm)... 

The most frequent elicitators of food allergy in children are peanuts and tree nuts [ 17]. In France the prevalence of food allergy has been estimated to be 3.2% [18]. Furthermore, in this study, food was identified as the most common cause of anaphylaxis. Here the major identified food allergens besides peanuts and tree nuts were shellfish, wheat and lupine flour [18]. 

AiTKEN s M, ATTUCCi s, IBRAHIM R K. and GULIK p J (1995) A cDNA encoding geranylgeranyl pyrophosphate synthase from white lupin . Plant Physiol, 108, 837-8. 

Membranes (50 pi in a total assay volume of 100 pi) were incubated with UDP-Gal (0.1 mM) and MgSO (10 mM) in 25 mM Tris-HCl buffer pH 7.5, for 10 or 60 min. Reactions were stopped by heating at 100°C for 3 min. Lupin galactan (0.1 mg) was added as a 0.1% solution, methanol was added to give a final concentration of 70% by volume, and the tubes were capped, heated at 70°C for 5 min and centrifuged (13000g 5 min). Supernatants were discarded or retained for analysis. Pellets were washed twice more with 70% methanol at 70 C and the supernatants were discarded. The final pellets were either dissolved in preparation for scintillation counting, or were suspended in water and freeze dried in preparation for analysis. 

Our standard incorporation assays contained resuspended particulate enzyme, labelled UDP-Gal (0.1 mM) and (10 mM) in resuspension buffer (Tris, pH 7.5). After incubation, reaction mixtures were heated briefly to 100°C and soluble lupin galactan was added, to ensure the precipitation of small amounts of galactan formed in the en me reaction and dissolved during the heating step. Precipitation of macromolecular products was achieved by adding methanol to a final concentration of 70%. The pellet was freed of soluble labelled products, including residual UDP-Gal, by repeated extraction with hot 70% methanol and was then analysed for labelled (l- )-P-D-galactan. The supernatant was analysed for soluble labelled products. 

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