Isoelectric focusing purity criteria and proton NMR detectable spectroscopic heterogeneity in the major isolated monomer hemoglobins from Glycera dibranchiata

Constantinidis, Ioannis; Satterlee, James D.

doi:10.1021/bi00398a037

Cited by 25 publications

(39 citation statements)

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“…A substantial body of chemical (Constantinidis et al, 1989;Constantinidis and Satterlee, 1987), spectroscopic (Kandler and Satterlee, 1983;Kandler et al, 1984;Constantinidis et al, 1988;Cooke and Wright, 1985a, b;Cooke et al, 1987), kinetic (Mintorovitch and Satterlee, 1988;Mintorovitch et al, 1989), and amino-terminal sequencing (Simons and Satterlee, 1989) knowledge has accumulated for the consistent preparation of the three major monomeric hemoglobin components from Glycera dibranchiata. These data confirm that these three monomeric components are unique proteins and not simply degradation products of a single protein.…”

Section: Resultsmentioning

confidence: 99%

“…The three major monomeric hemoglobins, labeled Components II-IV (GMH2, GMH3, and GMH4), all have molecular weights of about 16 kD (Kandler and Satterlee, 1983;Kandler et al, 1984). Isoelectric focusing (Constantinidis and Satterlee, 1987;Constantinidis et al, 1989) and amino-terminal sequencing of the wild-type proteins indicated the high purity and uniqueness of these individually isolated monomer hemoglobins (Simons and Satterlee, 1989). Similar advances in characterizing the polymeric hemoglobins have taken place recently (Zafar et al, 1990a, b).…”

Section: Introduction Smentioning

confidence: 83%

“…Hemoglobin was obtained from live bloodworms, Glycera dibranchiata, (Maine Bait Co., Newcastle, Maine) and separated into monomeric and polymeric fractions as described previously (Kandler et al, 1984;Constantinidis and Satterlee, 1987). Monomeric hemoglobin Component IV(GMH4) was separated from the other monomeric components using a cation exchange column (CM-Sepharose; Sigma) in which GMH4 was the final component eluted.…”

Section: Preparation Of Monomeric Hemoglobinmentioning

confidence: 99%

“…A major problem for those working with the Glycera dibranchiata monomer hemoglobins is that variations in isolation techniques, reproducibility, characterization, and purity assays in various laboratories makes comparing experimental results, and even correlating purified fractions, difficult (Arents and Love, 1989;Cooke and Wright, 1985a, b;Constantinidis and Satterlee, 1987;Harrington et al, 1978;Imamura et al, 1972;Kandler and Satterlee, 1983;Kandler et al, 1984;Li and Riggs, Parkhurst et al, 1980;Weber et al, 1977). As an illustration of the current state of difficulties, consider the status of protein primary sequences for these monomer hemoglobins.…”

Section: Introduction Smentioning

confidence: 99%

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Complete amino acid sequence of theGlycera dibranchiata monomer hemoglobin Component IV: Structural implications

1994

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The globin derived from the monomer Component IV hemoglobin of the marine amnelid, Glycera dibranchiata, has been completely sequenced, and the resulting information has been used to create a structural model of the protein. The most important result is that the consensus sequence of Component IV differs by 3 amino acids from a cDNA-predicted amino acid sequence thought earlier to encode the Component IV hemoglobin. This work reveals that the histidine (E7), typical of most heme-containing globins, is replaced by leucine in Component IV. Also significant is that this sequence is not identical to any of the previously reported Glycera dibranchiata monomer hemoglobin sequences, including the sequence from a previously reported crystal structure, but has high identity to all. A three-dimensional structural model for monomer Component IV hemoglobin was constructed using the published 1.5 A crystal structure of a monomer hemoglobin from Glycera dibranchiata as a template. The model shows several interesting features: (1) a Phe31 (B10) that is positioned in the active site; (2) a His39 occurs in an interhelical region occupied by Pro in 98.2% of reported globin sequences; and (3) a Met41 is found at a position that emerges from this work as a previously unrecognized heme contact.

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Section: Resultsmentioning

confidence: 99%

Section: Introduction Smentioning

confidence: 83%

Section: Preparation Of Monomeric Hemoglobinmentioning

confidence: 99%

Section: Introduction Smentioning

confidence: 99%

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Complete amino acid sequence of theGlycera dibranchiata monomer hemoglobin Component IV: Structural implications

1994

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“…Thus, La Mar and colleagues (Burns & La Mar, 1981), using NMR techniques, showed that the heme of tuna myoglobin has 2 different orientations present in a 60:40 ratio, similar to the distribution of the 2 forms of the D99K(P) mutant found in the present study. Cooke and Wright (1985) also reported a difference in heme orientation in the monomeric Hb of Glycera, and Constantinidis and Satterlee (1987) found that these forms were separable by isoelectric focusing. O'Connor et al (1980) and Santucci et al (1988) reported a correlation between heme orientation and circular dichroism in the Soret region of Glycera Hb.…”

Section: Circular Dichroism Spectramentioning

confidence: 94%

Properties of a recombinant human hemoglobin with aspartic acid 99 (β), an important intersubunit contact site, substituted by lysine

Yanase¹,

Cahill²,

Llano³

et al. 1994

Protein Science

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Site-directed mutagenesis of an important subunit contact site, , by a Lys residue (D99K(@)) was proven by sequencing the entire @-globin gene and the mutant tryptic peptide. Oxygen equilibrium curves of the mutant hemoglobin (Hb) (2-15 mM in heme) indicated that it had an increased oxygen affinity and a lowered but significant amount of cooperativity compared to native HbA. However, in contrast to normal HbA, oxygen binding of the recombinant mutant Hb was only marginally affected by the allosteric regulators 2,3-diphosphoglycerate or inositol hexaphosphate and was not at all responsive to chloride. The efficiency of oxygen binding by HbA in the presence of allosteric regulators was limited by the mutant Hb. At concentrations of 0.2 mM or lower in heme, the mutant D99K(@) Hb was predominantly a dimer as demonstrated by gel filtration, haptoglobin binding, fluorescence quenching, and light scattering. The purified dimeric recombinant Hb mutant exists in 2 forms that are separable on isoelectric focusing by about 0.1 pH unit, in contrast to tetrameric hemoglobin, which shows 1 band. These mutant forms, which were present in a ratio of 60:40, had the same masses for their heme and globin moieties as determined by mass spectrometry. The elution positions of the a-and @-globin subunits on HPLC were identical. Circular dichroism studies showed that one form of the mutant Hb had a negative ellipticity at 410 nm and the other had positive ellipticity at this wavelength. The findings suggest that the 2 D99K(@) recombinant mutant forms have differences in their heme-protein environments.

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Cushioning the pressure vibration of a zeolite concentrator system using a decoupled balancing duct system

Chang¹,

Lin²

2007

Environ. Prog.

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A honeycomb Zeolite Rotor Concentrator (HZRC) is the main air pollution control device utilized by many semiconductor and optoelectronics manufacturers. Various plant exhaust streams are collected and then transferred to the HZRC for decontamination. In a conventional HZRC, the exhaust fan movement and the switching between different air ducts can cause significant duct pressure variations resulting in production interruption. The minimization of pressure fluctuations to ensure continuous operation of production lines while maintaining a high volatile organic compounds (VOCs) removal efficiency is essential for exhaust treatment in these high technology manufactures. The article introduces a decoupled balancing duct system (DBDS) for controlling the airflows to achieve a balanced pressure in the HZRC system by adding a flow rate control device to the VOCs loaded stream bypass duct of a conventional system. Performance comparisons of HZRC with DBDS and other air flow control systems used by the wafer manufacturers in Hsinchu Science Park, Taiwan are presented. DBDS system had been proved effectively to stabilize the pressure in the airflow ducts, and thus avoided pressure fluctuations; it helped to achieve a high VOCs removal efficiency while ensuring the stability of the HZRC.

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Isoelectric focusing purity criteria and proton NMR detectable spectroscopic heterogeneity in the major isolated monomer hemoglobins from Glycera dibranchiata

Cited by 25 publications

References 23 publications

Complete amino acid sequence of theGlycera dibranchiata monomer hemoglobin Component IV: Structural implications

Complete amino acid sequence of theGlycera dibranchiata monomer hemoglobin Component IV: Structural implications

Properties of a recombinant human hemoglobin with aspartic acid 99 (β), an important intersubunit contact site, substituted by lysine

Cushioning the pressure vibration of a zeolite concentrator system using a decoupled balancing duct system

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