Hematoxylin and eosin staining of representative white perch ovary tissue sections.

<p>Ovary tissues were sampled at four key time points across one reproductive year during (A) pre-vitellogenesis (PreVG), (B) early-vitellogenesis (EVG), (C) mid-vitellogenesis (MVG), and (D) post-vitellogenesis (PostVG). Scale bar is 500 microns.</p

Average survival duration of food-restricted white perch and striped bass larvae.

<p>Dashed boxes indicate approximate time of hatching (~2 days) and onset of first feeding (~4 days in white perch, ~8 days in striped bass). [Mansuetti, 1964; Eldridge, et al., 1981; North & Houde, 2003].</p

Confocal microscopy of anti-VtgC coupled to DyLight633.

<p>Confocal microscopy images of immunohistochemistry of mature female white perch ovary tissues across one reproductive year stained with anti-VtgC coupled to DyLight633: (A) pre-vitellogenic (PreVG), (B) early-vitellogenic (EVG), (C) mid-vitellogenic (MVG), and (D) post-vitellogenic (PostVG) ovary sections.</p

VtgC affinity purification coupled to tandem mass spectrometry.

<p>VtgC affinity purification coupled to tandem mass spectrometry.</p

Sexually mature female white perch sampling statistics.

<p>Sexually mature female white perch sampling statistics.</p

White perch LR8 and Lrp13 western blotting.

<p>Results of western blotting for the two white perch vitellogenin receptors in female liver, plasma, and ovary tissues sampled across one reproductive year during pre-vitellogenesis (PreVG), early-vitellogenesis (EVG), mid-vitellogenesis (MVG), and post-vitellogenesis (PostVG) across three biological replicates.</p

White perch vitellogenin Aa, Ab, and C western blotting.

<p>Results of western blotting for the three white perch vitellogenins in female liver, plasma, and ovary tissues sampled across one reproductive year during pre-vitellogenesis (PreVG), early-vitellogenesis (EVG), mid-vitellogenesis (MVG), and post-vitellogenesis (PostVG) pooled from three individuals at each time point.</p

Vitellogenin composition in white perch and striped bass egg yolk.

<p>In white perch (<i>M</i>. <i>americana</i>), yolk proteins derived from VtgC are minor components of the total egg yolk (< 5%), whereas in striped bass (<i>M</i>. <i>saxatilis</i>) they are major components of the egg yolk (~ 25%). [Williams et al., 2014 (J Exp Zool Part A); Schilling et al., 2014 (J Proteome Res)].</p

Protein cleavage-isotope dilution mass spectrometry (PC-IDMS) tandem mass spectrometry results for the three white perch vitellogenins (VtgAa, VtgAb, and VtgC).

<p>Results from protein cleavage-isotope dilution mass spectrometry (PC-IDMS) tandem mass spectrometry for the three white perch vitellogenins (VtgAa, VtgAb, and VtgC) in female liver, plasma, and ovary tissues sampled across one reproductive year during pre-vitellogenesis (PreVG), early-vitellogenesis (EVG), mid-vitellogenesis (MVG), and post-vitellogenesis (PostVG) across 3 biological replicates. The mean ± SD is shown. “N.Q.” indicates that the native peptide was not quantifiable. Levels not connected by the same letter are significantly different at α = 0.05.</p

Enzyme-Modified Carbon-Fiber Microelectrode for the Quantification of Dynamic Fluctuations of Nonelectroactive Analytes Using Fast-Scan Cyclic Voltammetry

Neurotransmission occurs on a millisecond time scale, but conventional methods for monitoring nonelectroactive neurochemicals are limited by slow sampling rates. Despite a significant global market, a sensor capable of measuring the dynamics of rapidly fluctuating, nonelectroactive molecules at a single recording site with high sensitivity, electrochemical selectivity, and a subsecond response time is still lacking. To address this need, we have enabled the real-time detection of dynamic glucose fluctuations in live brain tissue using background-subtracted, fast-scan cyclic voltammetry. The novel microbiosensor consists of a simple carbon fiber surface modified with an electrodeposited chitosan hydrogel encapsulating glucose oxidase. The selectivity afforded by voltammetry enables quantitative and qualitative measurements of enzymatically generated H₂O₂ without the need for additional strategies to eliminate interfering agents. The microbiosensors possess a sensitivity and limit of detection for glucose of 19.4 ± 0.2 nA mM^–1 and 13.1 ± 0.7 μM, respectively. They are stable, even under deviations from physiological normoxic conditions, and show minimal interference from endogenous electroactive substances. Using this approach, we have quantitatively and selectively monitored pharmacologically evoked glucose fluctuations with unprecedented chemical and spatial resolution. Furthermore, this novel biosensing strategy is widely applicable to the immobilization of any H₂O₂ producing enzyme, enabling rapid monitoring of many nonelectroactive enzyme substrates