Literature DB >> 24307125

Potentially defensive proteins in mature seeds of 59 species of tropical leguminosae.

D H Janzen1, C A Ryan, I E Liener, G Pearce.   

Abstract

A survey of 59 species of tropical legume seeds revealed high interspecific variation in proteinaceous capacity to inhibit bovine trypsin (a digestive enzyme) and to agglutinate human (type B, Rh positive) and laboratory rabbit red blood cells. The legume subfamily Mimosoideae was conspicuous for the absence of seeds with very weak trypsin inhibition. Congenerics sometimes differed strongly from each other with respect to both trypsin inhibition and phytohemagglutination. Half the species of seeds displayed no hemagglutinating capacity with one or the other kinds of red blood cells, and in only 27% of the 30 cases where there was some activity did the same species of seed actively agglutinate both species of red blood cells. A species of seed that had hemagglutinating capacity was almost invariably associated with moderate to high levels of trypsin inactivation. While it has been long known that a great diversity of small toxic and potentially defensive molecules occur in legume seeds and that one species of seed often contains several of them, we now feel that it is reasonable to consider legume seeds as also containing a high diversity of potentially toxic protein molecules. A single seed is likely to contain, at the least, three to four classes of defensive compounds, any or all of which, or some in combination, may be the cause of a seed being rejected by a potential seed predator.

Entities:  

Year:  1986        PMID: 24307125     DOI: 10.1007/BF01012365

Source DB:  PubMed          Journal:  J Chem Ecol        ISSN: 0098-0331            Impact factor:   2.626


  16 in total

1.  1,4-Butanediol diglycidyl ether coupling of carbohydrates to Sepharose: affinity adsorbents for lectins and glycosidases.

Authors:  R Uy; F Wold
Journal:  Anal Biochem       Date:  1977-07       Impact factor: 3.365

2.  A modified spectrophotometric determination of chymotrypsin, trypsin, and thrombin.

Authors:  B C HUMMEL
Journal:  Can J Biochem Physiol       Date:  1959-12

3.  The photometric determination of the hemagglutinating activity of soyin and crude soybean extracts.

Authors:  I E LIENER
Journal:  Arch Biochem Biophys       Date:  1955-01       Impact factor: 4.013

4.  p-Nitrophenyl-p'-guanidinobenzoate HCl: a new active site titrant for trypsin.

Authors:  T Chase; E Shaw
Journal:  Biochem Biophys Res Commun       Date:  1967-11-30       Impact factor: 3.575

5.  Studies on the proteins from the seeds of Croton tiglium and of Jatropha curcas. Toxic properties and inhibition of protein synthesis in vitro.

Authors:  F Stirpe; A Pession-Brizzi; E Lorenzoni; P Strocchi; L Montanaro; S Sperti
Journal:  Biochem J       Date:  1976-04-15       Impact factor: 3.857

6.  Utilization by chicks of half-cystine from native and denatured proteinase inhibitor protein from potatoes.

Authors:  G Pearce; J McGinnis; C A Ryan
Journal:  Proc Soc Exp Biol Med       Date:  1979-02

7.  Toxic effects of Jatropha curcas in mice.

Authors:  S E Adam
Journal:  Toxicology       Date:  1974-03       Impact factor: 4.221

Review 8.  Protein inhibitors of proteinases.

Authors:  M Laskowski; I Kato
Journal:  Annu Rev Biochem       Date:  1980       Impact factor: 23.643

9.  Ammonia utilization by the bruchid beetle,Caryedes brasiliensis [Bruchidae].

Authors:  G A Rosenthal; D H Janzen
Journal:  J Chem Ecol       Date:  1985-04       Impact factor: 2.626

10.  Insecticidal action of the phytohemagglutinin in black beans on a bruchid beetle.

Authors:  D H Janzen; H B Juster; I E Liener
Journal:  Science       Date:  1976-05-21       Impact factor: 47.728

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  1 in total

1.  Quinolizidine alkaloids in Ormosia arborea seeds inhibit predation but not hoarding by agoutis (Dasyprocta leporina).

Authors:  Paulo Roberto Guimarães; Juliana José; Mauro Galetti; José Roberto Trigo
Journal:  J Chem Ecol       Date:  2003-05       Impact factor: 2.626

  1 in total

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