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  • Brand : BIOFRON

  • Catalogue Number : BN-O1148

  • Specification : 98%(HPLC)

  • CAS number : 4149-06-8

  • Formula : C9H9N3O

  • Molecular Weight : 175.19

  • Volume : 5mg

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Catalogue Number


Analysis Method





Molecular Weight



Botanical Source

Structure Type










Flash Point


Boiling Point

312.3ºC at 760mmHg

Melting Point

210-215 °C (dec.)(lit.)


InChl Key

WGK Germany


HS Code Reference

Personal Projective Equipment

Correct Usage

For Reference Standard and R&D, Not for Human Use Directly.

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provides coniferyl ferulate(CAS#:4149-06-8) MSDS, density, melting point, boiling point, structure, formula, molecular weight etc. Articles of coniferyl ferulate are included as well.>> amp version: coniferyl ferulate

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The aim of this study was to determine the response of photosynthetic carbon metabolism in spinach and bean to low temperature. (a) Exposure of warm-grown spinach and bean plants to 10°C for 10 days resulted in increases in the total activities of a number of enzymes, including ribulose 1,5-bisphosphate carboxylase (Rubisco), stromal fructose 1,6 bisphosphatase (Fru 1,6-P2ase), sedoheptulose 1,7-bisphosphatase (Sed 1,7-P2ase), and the cytosolic Fru 1,6-P2ase. In spinach, but not bean, there was an increase in the total activity of sucrose-phosphate synthase. (b) The CO2-saturated rates of photosynthesis for the cold-acclimated spinach plants were 68% greater at 10°C than those for warm-acclimated plants, whereas in bean, rates of photosynthesis at 10°C were very low after exposure to low temperature. (c) When spinach leaf discs were transferred from 27 to 10°C, the stromal Fru 1,6-P2ase and NADP-malate dehydrogenase were almost fully activated within 8 minutes, and Rubisco reached 90% of full activation within 15 minutes of transfer. An initial restriction of Calvin cycle fluxes was evident as an increase in the amounts of ribulose 1,5-bisphosphate, glycerate-3-phosphate, Fru 1,6-P2, and Sed 1,7-P2. In bean, activation of stromal Fru 1,6-P2ase was weak, whereas the activation state of Rubisco decreased during the first few minutes after transfer to low temperature. However, NADP-malate dehydrogenase became almost fully activated, showing that no loss of the capacity for reductive activation occurred. (d) Temperature compensation in spinach evidently involves increases in the capacities of a range of enzymes, achieved in the short term by an increase in activation state, whereas long-term acclimation is achieved by an increase in the maximum activities of enzymes. The inability of bean to activate fully certain Calvin cycle enzymes and sucrose-phosphate synthase, or to increase nonphotochemical quenching of chlorophyll fluorescence at 10°C, may be factors contributing to its poor performance at low temperature.


Changes in Activities of Enzymes of Carbon Metabolism in Leaves during Exposure of Plants to Low Temperature 1


A. Scott Holaday, Wayne Martindale, Rhu Alred, Andrew L. Brooks, and Richard C. Leegood

Publish date

1992 Mar




We tested the possibility that two phenotypic traits, defective activation of macrophage antileishmanial activities and susceptibility to infection with Leishmania major, were controlled by the same gene. We used P/J (susceptible) and C3H/HeN (resistant) mice to breed F1, backcross (Bx), and F2 mice that were tested individually for both traits, each of which is known to be controlled by a single autosomal gene. We found no correlation between the macrophage defect and cutaneous disease. There was a correlation between development of systemic disease and defective macrophage activation in Bx mice; this correlation, however, was not confirmed in the F2 population.


Susceptibility of inbred mice to Leishmania major infection: genetic analysis of macrophage activation and innate resistance to disease in individual progeny of P/J (susceptible) and C3H/HeN (resistant) mice.


A H Fortier, A Tong, and C A Nacy

Publish date

1990 Dec;




Mammalian reproduction is dependent upon intermittent delivery of luteinizing hormone-releasing hormone (LHRH) to the anterior pituitary. This mode of secretion is required to sensitize maximally the gonadotrophs to LHRH stimulation and to regulate gonadotropin gene expression. While LHRH secretion is pulsatile in nature, the origin of the pulse generator is unknown. In this report, we show that this oscillator could be located within the LHRH neuronal network. When immortalized LHRH neurons are placed into a perifusion system, LHRH is secreted into the medium in a pulsatile fashion under basal conditions. LHRH secretion and the number of LHRH pulses are reduced when calcium is removed from the medium. Perifusion also influences pro-LHRH processing, since the molar ratio of its processed products varies dramatically when the cells are transferred from a static system. Several different cellular mechanisms may underlie these changes in secretion and processing. Lucifer yellow experiments reveal that some cells are dye-coupled. Hence, these cells could be electrically coupled through gap junctions such that secretion from individual cells could be coordinated. Secretion could also be synchronized through the observed synapse-like contacts. These contacts could perform a negative-feedback role to regulate not only the amount of LHRH released but also the molecular forms secreted. The organization of LHRH neurons into interconnected clusters could serve to coordinate LHRH secretion from individual cells and, thereby, orchestrate functions in vivo as diverse as the onset of puberty, the timing of ovulation, and the duration of lactational infertility


Intrinsic pulsatile secretory activity of immortalized luteinizing hormone-releasing hormone-secreting neurons.


W C Wetsel, M M Valenca, I Merchenthaler, Z Liposits, F J Lopez, R I Weiner, P L Mellon, and A Negro-Vilar

Publish date

1992 May 1;

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