Literature DB >> 16668362

Two kunitz-type proteinase inhibitors from potato tubers.

T A Walsh1, W P Twitchell.   

Abstract

Two proteinase inhibitors have been isolated from tubers of potato (Solanum tuberosum). Based on N-terminal amino acid sequence homologies, they are members of the Kunitz family of proteinase inhibitors. Potato Kunitz inhibitor-1 (molecular weight 19,500, isoelectric point 6.9) is a potent inhibitor of the animal pancreatic proteinase trypsin, and its amino terminus has significant homology to a recently characterized cathepsin D Kunitz inhibitor from potato tubers (Mares et al. [1989] FEBS Lett 251:94-98). Potato Kunitz inhibitor-2 (molecular weight 20,500, isoelectric point 8.6) is an inhibitor of the microbial proteinase subtilisin Carlsberg; its amino terminus is almost identical to an abundant 22 kilodalton protein from potato tubers (Suh et al. [1990] Plant Physiol 94:40-45) and has significant homology to other Kunitz-type subtilisin inhibitors from small grains. Both Kunitz inhibitors are abundant proteins of the cortex of potato tubers.

Entities:  

Year:  1991        PMID: 16668362      PMCID: PMC1080957          DOI: 10.1104/pp.97.1.15

Source DB:  PubMed          Journal:  Plant Physiol        ISSN: 0032-0889            Impact factor:   8.340


  14 in total

1.  Naturally occurring protein crystals in the potato : inhibitor of papain, chymopapain, and ficin.

Authors:  P Rodis; J E Hoff
Journal:  Plant Physiol       Date:  1984-04       Impact factor: 8.340

2.  A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding.

Authors:  M M Bradford
Journal:  Anal Biochem       Date:  1976-05-07       Impact factor: 3.365

3.  Isolation of a carboxypeptidase B inhibitor from potattoes.

Authors:  J M Rancour; C A Ryan
Journal:  Arch Biochem Biophys       Date:  1968-04       Impact factor: 4.013

4.  Comparative study on amino acid sequences of Kunitz-type soybean trypsin inhibitors, Tia, Tib, and Tic.

Authors:  S H Kim; S Hara; S Hase; T Ikenaka; H Toda; K Kitamura; N Kaizuma
Journal:  J Biochem       Date:  1985-08       Impact factor: 3.387

5.  Chymotrypsin inhibitor I from potatoes. Large scale preparation and characterization of its subunit components.

Authors:  J C Melville; C A Ryan
Journal:  J Biol Chem       Date:  1972-06-10       Impact factor: 5.157

6.  Isolation and characterization of a proteinaceous inhibitor of microbial proteinases induced during the hypersensitive reaction of tobacco to tobacco mosaic virus.

Authors:  P Geoffroy; M Legrand; B Fritig
Journal:  Mol Plant Microbe Interact       Date:  1990 Sep-Oct       Impact factor: 4.171

7.  Purification and characterization of the 22-kilodalton potato tuber proteins.

Authors:  S G Suh; J E Peterson; W J Stiekema; D J Hannapel
Journal:  Plant Physiol       Date:  1990-09       Impact factor: 8.340

8.  Proteinase inhibitor II from potatoes: isolation and characterization of its protomer components.

Authors:  J Bryant; T R Green; T Gurusaddaiah; C A Ryan
Journal:  Biochemistry       Date:  1976-08-10       Impact factor: 3.162

9.  Amino acid sequences of two trypsin inhibitors from winged bean seeds (Psophocarpus tetragonolobus (L)DC.).

Authors:  M Yamamoto; S Hara; T Ikenaka
Journal:  J Biochem       Date:  1983-09       Impact factor: 3.387

10.  The complete amino acid sequence of trypsin inhibitor DE-3 from Erythrina latissima seeds.

Authors:  F J Joubert; C Heussen; E B Dowdle
Journal:  J Biol Chem       Date:  1985-10-25       Impact factor: 5.157

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  11 in total

1.  Potato cysteine proteinase inhibitor gene family: molecular cloning, characterisation and immunocytochemical localisation studies.

Authors:  K Gruden; B Strukelj; M Ravnikar; M Poljsak-Prijatelj; I Mavric; J Brzin; J Pungercar; I Kregar
Journal:  Plant Mol Biol       Date:  1997-05       Impact factor: 4.076

2.  Defense response in non-genomic model species: methyl jasmonate exposure reveals the passion fruit leaves' ability to assemble a cocktail of functionally diversified Kunitz-type trypsin inhibitors and recruit two of them against papain.

Authors:  Sylvio Botelho-Júnior; Olga L T Machado; Kátia V S Fernandes; Francisco J A Lemos; Viviane A Perdizio; Antônia E A Oliveira; Leandro R Monteiro; Mauri L Filho; Tânia Jacinto
Journal:  Planta       Date:  2014-05-22       Impact factor: 4.116

3.  A novel function for the cathepsin D inhibitor in tomato.

Authors:  Purificación Lisón; Ismael Rodrigo; Vicente Conejero
Journal:  Plant Physiol       Date:  2006-09-29       Impact factor: 8.340

4.  Detection of immunologically related Kunitz and Bowman-Birk proteinase inhibitors expressed during potato tuber development.

Authors:  C Mitsumori; K Yamagishi; K Fujino; Y Kikuta
Journal:  Plant Mol Biol       Date:  1994-11       Impact factor: 4.076

5.  Zebra chip disease decreases tuber (Solanum tuberosum L.) protein content by attenuating protease inhibitor levels and increasing protease activities.

Authors:  G N Mohan Kumar; Lisa O Knowles; N Richard Knowles
Journal:  Planta       Date:  2015-06-20       Impact factor: 4.116

6.  Functional comparison of homologous members of three groups of Kunitz-type enzyme inhibitors from potato tubers (Solanum tuberosum L.).

Authors:  A Heibges; F Salamini; C Gebhardt
Journal:  Mol Genet Genomics       Date:  2003-05-29       Impact factor: 3.291

7.  Structural diversity and organization of three gene families for Kunitz-type enzyme inhibitors from potato tubers (Solanum tuberosum L.).

Authors:  A Heibges; H Glaczinski; A Ballvora; F Salamini; C Gebhardt
Journal:  Mol Genet Genomics       Date:  2003-05-29       Impact factor: 3.291

8.  Isolation and sequence analysis of the genomic DNA fragment encoding an aspartic proteinase inhibitor homologue from potato (Solanum tuberosum L.).

Authors:  D B Maganja; B Strukelj; J Pungercar; F Gubensek; V Turk; I Kregar
Journal:  Plant Mol Biol       Date:  1992-10       Impact factor: 4.076

9.  Jasmonic acid-inducible gene expression of a Kunitz-type proteinase inhibitor in potato tuber disks.

Authors:  K Yamagishi; C Mitsumori; K Takahashi; K Fujino; Y Koda; Y Kikuta
Journal:  Plant Mol Biol       Date:  1993-02       Impact factor: 4.076

10.  A chickpea Kunitz trypsin inhibitor is located in cell wall of elongating seedling organs and vascular tissue.

Authors:  Teresa Jiménez; Ignacio Martín; Emilia Labrador; Berta Dopico
Journal:  Planta       Date:  2007-01-17       Impact factor: 4.540

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