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Category:Vehicle wiring
Category:Electronic vehicle control systemsCircular dichroism and fluorescence studies of catecholase-type C79-hemocyanin from the cyanobacterium Synechococcus elongatus strain PCC 7942.
A catecholase-type C(2)a(2)a(2) hemocyanin from the cyanobacterium Synechococcus elongatus strain PCC 7942 (SCC7942) was purified and characterized. The SCC7942 hemocyanin is very similar to Trp-containing, mainly alpha(2) (C(2)a(2)a(2) fold) catecholases such as MSP-chDox, type 3, respectively Trp-Tyr, in all aspects studied. The hemocyanin of strain SCC7942 contained 46+/-1.4 residues of globin and 29+/-3.0 residues of capping protein per mol of beta(2) chain, which is in agreement with the two beta(2) chains (29.3 kDa) that resulted from mass spectroscopy. Circular dichroism and fluorescence studies on both the SCC7942 hemocyanin and its apoprotein showed that neither the apoprotein nor the holo-hemocyanin contain significant amounts of intrinsic or extrinsic fluorescence of tryptophan residues. Thus, both the apoprotein and the holo-hemocyanin lack tryptophan fluorescence and the conformational changes involved in the ligand binding do not involve a decrease in the quenching efficiency of tryptophan residues. The effect of different concentrations of copper was studied by determining the number of tyrosyl residues on the beta(2) subunit and by CD measurements. The results showed that the lowest amount of copper in the holo-hemocyanin was within the range of that found to induce ligand binding.Index, key, value string) {
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Category: ECU (control unit)Please see attached.

“Nick Papadakis” on 12/14/2000 07:18:40 PM
To: “”
Subject: FW: PG&E Open Season


Here’s the blustery Nickels to send to you via email. He said we should be
kind to these guys (who are trying to help the state get some “liquidity”
moving forward).


—–Original Message—–
From: “Nick Papadakis” @ENRON
Sent: Tuesday, December 12, 2000 4:54 PM
Subject: PG&E Open Season

Dear Fellow

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