Claim · model-written summary
Azocollase B has a pI of 9.0.
- Taxon
- Soybean
Glycine maxt0 - Gene
- Azocollase Be1
- Outcome
- pIe1
- Value
- 9.0e1
Not reportedMaterialCompoundOrgan / stageInteractorInteractor roleSecond interactorSecond interactor roleTreatmentComparatorSettingDirectionQualifier
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
t0“Soybean”
e1“Azocollase B has a molecular weight of 52,000 and a pI of 9.0”
Title
Azocoll-digesting Proteinases in Soybean Leaves
La Verne Ragster; Maarten J. Chrispeels PLANT PHYSIOLOGY 1979. doi:10.1104/pp.64.5.857
Other claims from this paper (17)
- Observation Two different endopeptidases that digest the chromogenic substrate Azocoll were found in soybean leaves.
- Observation Azocollase A has a molecular weight of 17,500.
- Observation Azocollase A has a pI of 6.0.
- Observation Azocollase B has a molecular weight of 52,000.
- Observation Both azocollases digest Azocoll optimally at pH 9.0.
- Intervention effect Azocollase A is inhibited by 3 millimolar EDTA.
- Intervention effect Azocollase B is inhibited by 100 micromolar parachloromercuribenzoate.
- Observation Total azocollase activity gradually increased during leaf maturation, when leaf protein and chlorophyll increased.
- Observation Total azocollase activity then declined again during leaf senescence.
- Observation Young leaves that are still expanding contain mostly azocollase B and little azocollase A.
- Observation Leaf maturation was associated with a dramatic 40- to 50-fold increase in azocollase A, which occurred in the 2- to 3-week period following leaf expansion.
- Observation During leaf maturation azocollase B activity increased more slowly than azocollase A.
- Observation Azocollase A, separated from other proteinases by gel filtration, digested denatured leaf protein and casein, releasing free alpha-amino groups.
- Observation Autodigestion of leaf extracts at pH 9.0 broke down leaf proteins, releasing free alpha-amino groups and causing endopeptidic cleavage of polypeptides.
- Intervention effect Polypeptide cleavage in leaf extracts was not inhibited by parachloromercuribenzoate.
- Intervention effect Polypeptide cleavage in leaf extracts was not inhibited by EDTA.
- Mechanism The authors concluded that the azocollases do not play a major role in the hydrolysis of leaf proteins in crude extracts.