Literature DB >> 16658230

Immunological Comparisons of Chymotrypsin Inhibitor I among Several Genera of the Solanaceae.

S Gurusiddaiah1, T Kuo, C A Ryan.   

Abstract

Microcomplement fixation was employed to compare the immunological differences that occur between purified inhibitor I from potato tubers, the four purified protomers that comprise it, and inhibitor I from tuber and leaf extracts. Total inhibitors of chymotrypsin and trypsin in leaves of seven genera of the Solanaceae were identified by enzymatic assay. In leaves of three genera, Solanum, Lycopersicum, and Datura, chymotrypsin inhibitor I was identified immunologically. In petals of all seven genera inhibitor I was also identified immunologically. With the microcomplement fixation technique inhibitor I from leaf or petal extracts of eight Solanaceae genera were compared. An immunological relationship of inhibitor I among seven of these genera was established.

Entities:  

Year:  1972        PMID: 16658230      PMCID: PMC366203          DOI: 10.1104/pp.50.5.627

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


  10 in total

1.  CONCERNING A CRYSTALLINE CHYMOTRYPTIC INHIBITOR FROM POTATOES, AND ITS BINDING CAPACITY FOR THE ENZYME.

Authors:  A K BALLS; C A RYAN
Journal:  J Biol Chem       Date:  1963-09       Impact factor: 5.157

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

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

3.  An inducible protein in potato and tomato leaflets.

Authors:  C A Ryan
Journal:  Plant Physiol       Date:  1968-11       Impact factor: 8.340

4.  Protein measurement with the Folin phenol reagent.

Authors:  O H LOWRY; N J ROSEBROUGH; A L FARR; R J RANDALL
Journal:  J Biol Chem       Date:  1951-11       Impact factor: 5.157

5.  Immunological time scale for hominid evolution.

Authors:  V M Sarich; A C Wilson
Journal:  Science       Date:  1967-12-01       Impact factor: 47.728

6.  Synthesis of chymotrypsin inhibitor I protein in potato leaflets induced by detachment.

Authors:  C A Ryan
Journal:  Plant Physiol       Date:  1968-11       Impact factor: 8.340

7.  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

8.  The dependence of immunological cross-reactivity upon sequence resemblance among lysozymes. II. Comparison of precipitin and micro-complement fixation results.

Authors:  E M Prager; A C Wilson
Journal:  J Biol Chem       Date:  1971-11-25       Impact factor: 5.157

9.  Transitory Aspects of a Single Protein in Tissues of Solanum tuberosum and Its Coincidence With the Establishment of New Growth.

Authors:  C A Ryan; O C Huisman; R W Van Denburgh
Journal:  Plant Physiol       Date:  1968-04       Impact factor: 8.340

10.  Wound-Induced Proteinase Inhibitor in Plant Leaves: A Possible Defense Mechanism against Insects.

Authors:  T R Green; C A Ryan
Journal:  Science       Date:  1972-02-18       Impact factor: 47.728

  10 in total
  4 in total

1.  Molecular characterization of a wound-inducible inhibitor I gene from potato and the processing of its mRNA and protein.

Authors:  T E Cleveland; R W Thornburg; C A Ryan
Journal:  Plant Mol Biol       Date:  1987-05       Impact factor: 4.076

2.  Wound-induced Accumulation of Trypsin Inhibitor Activities in Plant Leaves: Survey of Several Plant Genera.

Authors:  M Walker-Simmons; C A Ryan
Journal:  Plant Physiol       Date:  1977-03       Impact factor: 8.340

3.  Assay and Biochemical Properties of the Proteinase Inhibitor-inducing Factor, a Wound Hormone.

Authors:  C A Ryan
Journal:  Plant Physiol       Date:  1974-09       Impact factor: 8.340

4.  Constitutive and jasmonate-inducible traits of Datura wrightii.

Authors:  J Daniel Hare; Linda L Walling
Journal:  J Chem Ecol       Date:  2006-02-26       Impact factor: 2.626

  4 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.