Compressibility and specific volume of actin decrease upon G to F transformation

We measured the densities as well as the sound velocities in solutions of G-actin, F-actin and the reconstituted thin filament. Using the data obtained, we determined their partial specific volumes and partial specific adiabatic compressibilities. The objectives were to investigate the volume change of actin upon polymerization and to detect the conformational change associated with the Ca²⁺-binding to the reconstituted thin filament. The partial specific volume and the partial specific adiabatic compressibility of G-actin were 0.749 cm³/g and 9.3 · 10⁻¹² cm²/dyne, respectively. The results suggest that G-actin is a rather soft protein compared with other globular proteins. The partial specific volumes of F-actin were in a range of 0.63–0.66 cm³/g depending on the solvent conditions. The partial specific adiabatic compressibilities of F-actin were negative (−(7–13) · 10⁻¹² cm³/dyne). These data indicate that the amount of hydration may increase by several times upon polymerization assuming that the size of the cavity remains constant. We detected little difference between the partial specific adiabatic compressibility of the reconstituted thin filament in a Ca²⁺-bound state and that in a Ca²⁺-unbound state. This suggests that the Ca²⁺ binding affected not the subunit itself but the inter-subunit junction.     

Physicochemical studies of oligodextran. I. Molecular weight dependence of intrinsic viscosity, partial specific compressibility and hydrated water

The number average molecular weight, Mn, of low molecular weight dextran was determined through endgroup analysis, and the intrinsic, viscosities of these materials in aqueous solution were determined at 25°C. The ultrasonic velocities in their aqueous solutions were also measured at 25 and 45°C. As concerns the molecular weight dependence of the intrinsic viscosity, partial specific compressibility of solute and the hound water around the solute, the following results were obtained. (1) log [η]-log Mn and [η]/Mn^0.5 – Mn^0.5 plots were in accord with the Mark-Houwink and Stockmayer-Fix-man equations respectively for Mn > 2, 000, but these plots deviated from the equations for Mn < 2, 000. (2)The partial specific compressibility, β ₁°, of dextran is expressed by following equation for Mn < 2,000: β ₁° = 10^?12 × (13.6 log Mn - 51.7) (cm²/dyne). In contrast, it, becomes the constant value, -- 7.3 × 10^?12 cm²/dyne, for Mn > 2,000. (3) The amount of bound water of dextran calculated from the sound velocity measurement lakes constant value of 0.17 ml g for Mn > 2, 000, but the amount of hydration increase with decreasing molecular weight for Mn < 2,000. From these results, a dextran molecule in aqueous solution is expected to change its conformation from random coiling to uncoiling stretched form at the molecular weight of around 2, 000 or about 12 glucose units.     

Implications of Using Steady-State Conditions in Estimating Dermal Uptake of Volatile Compounds in Municipal Drinking Water: An Example of THMs

Dermal exposure to volatile compounds (VC) in municipal water while showering is typically estimated using a steady-state condition between VC in water impacting on skin and skin exposed to water. The lag times to achieve steady-state between VC and skin can vary in the range of 7.5–218.3 min, while shower duration is often less than these values. Estimates of dermal exposure to VC using steady-state while showering may misinterpret exposure. This study developed models and estimated exposure to some disinfection byproducts (DBPs) through dermal pathway by considering lag times while showering. Dermal uptakes of VC were compared using different approaches. In the proposed approach, uptakes of trihalomethanes were estimated between 9.55 × 10^?10–1.43 × 10^?8 mg/cm² of skin during the lag times from exposure to water with trihalomethanes of 50 μg/L. These values were higher than the steady-state estimates (1.37 × 10^?10–4.34 × 10^?9 mg/cm²), and lower than the average exposure analysis (4.12 × 10^-8–1.93 × 10^?6 mg/cm²). Using the Drinking Water Surveillance Program data in Ontario, chronic daily intakes of trihalomethanes were estimated to be 9.40 × 10^?7 (1.85 × 10^?7–1.65 × 10^?6), 3.89 × 10^?6 (7.11 × 10^?7–2.33 × 10^?5), and 1.40 × 10^?6 (4.0 × 10^?7–1.77 × 10^?6) mg/kg/day in Toronto, Ottawa, and Hamilton, respectively. The findings can be useful in understanding THMs exposure and risk through dermal pathway.     

Low Values of the Scheraga–Mandelkern β parameter for proteins. An explanation based on porous sphere hydrodynamics

Several globular proteins have values of the Scheraga–Mandelkern β parameter significantly below the theoretical minimum value, β₀ = 2.112 × 10⁶, for an impermeable sphere. Using the Felderhof–Deutch generalization of the Debye–Bueche–Brinkman theory of hydrodynamics of porous spheres, we have shown that values of β slightly below this supposed minimum are theoretically expected. A porous sphere of uniform density has a minimum β of 2.084 × 10⁶ at a Debye shielding ratio of 6.5, corresponding, for example, to a sphere radius of 11 Å and an inverse hydrodynamic shielding length of 0.6 Å^?1, values not far from those of small proteins. A two-layer porous sphere model gives similar results. Although this is the first theoretical explanation of values of β below β₀, the theory is incomplete since β values as low as 2.03 × 10⁶ are observed.     

Conformational deformation in deoxymyoglobin by hydrostatic pressure

Pressure effect on the equilibrium conformation in sperm whale deoxymyoglobin and its volume fluctuation are studied by the normal mode analysis and strain tensor analysis. The pressure-induced deformation of interhelix regions are found to be remarkably more compressed than the other parts of the molecule. The intrahelix compressibility is shown to be relatively small. We also calculate the compressibility of the three hydrophobic clusters, located at the bottom, distal, and proximal side of the heme. Its value is found to decrease in the indicated order. The average compressibility of these hydrophobic clusters is less than the average interhelix compressibility, even though there are large cavities in these clusters. In order to study overall deformation, we define a linear compressibility and calculate it for all pairs of C^αatoms. The pressure-induced deformation is observed to be heterogeneous also in this analysis. The calculated root-mean-square displacement of the constituent atoms in the equilibrium conformation at 1,000 atm from those at 0 atm is 0.12 Å, which is much smaller in magnitude than the average value of the atomic fluctuations at room temperature. In the water solvent, the volume excluded by the protein molecule in the equilibrium conformation is reduced by 0.9%, when the pressure is raised from 0 to 1,000 atm. The calculated magnitude of the root-mean-square volume fluctuation is 0.3% of the excluded volume at room temperature. The square of the volume fluctuation is given as a sum of contributions from individual normal modes. Contributions from low frequency normal modes are found to dominate over those from higher frequency normal modes. The estimated value of the isothermal compressibility of deoxymyoglobin is 9.37 × 10^?12 cm²/dyn. © 1993 Wiley-Liss, Inc.     

Shape of the conformational energy surface near the global minimum and low-frequency vibrations in the native conformation of globular proteins

Based on the assumption that the conformational energy surface of a protein molecule can be approximated near the global minimum point by a multidimensional parabola, conformational fluctuations in the native state are discussed. In this approximation the conformational fluctuations can be viewed as excitations of coupled harmonic oscillations of dihedral angles. For the purpose of estimating the range of frequencies vibrations, globular proteins are assumed to made of homogeneous continuous elastic material. The number of vibrational modes in such an elastic body, with the wavelength no less than the characteristic length of an amino acid residue, are estimated roughly to be three times the number of amino acid residues in a protein, which is slightly less than the number of variable dihedral angles in a protein. Their frequencies, when converted to the wavenumber of corresponding light, are found to range from 1.8 × 10 cm^?1 to 2.1 × 10²cm^?1 for a protein with the diameter d = 40 Å, when Young's E = 10¹¹ dyne/cm² is assumed. A significant fraction of the coupled vibrations of dihedral angles in real globular proteins are collective ones, i.e., those involving the whole protein molecules. Based on these results, it concluded that the depth of the global minimum s at least 150 Kcal/mol.     

S-adenosylmethionine: Protein-carboxyl methyltransferase from erythrocyte

Protein methylase II (S-adenosylmethionine:protein—carboxyl methyltrans-ferase), which modifies free carboxyl residues of protein, was purified from both rat and human blood, and properties of the enzymes were studied. The pH optima for the reaction were dependent on the substrate proteins used; pH 7.0 was found with endogenous substrate, 6.1 with plasma, 6.5 with γ-globulin, and 6.0 with fibrinogen. The molecular weight of the enzymes from both rat and human erythrocytes were identical (25,000 daltons) determined by Sephadex G-75 chromatography. Partially purified enzyme from rat erythrocytes showed three peaks on electrofocusing column at pH 4.9, 5.5 and 6.0. The K_m values of the enzymes from rat and human erythrocytes showed 3.1 × 10^?6m and 1.92 × 10^?6m at pH 6.0, 1.96 × 10^?6m and 1.78 × 10^?6m at pH 7.2, respectively, for S-adenosyl-l-methionine. It is also found that S-adenosyl-l-homocysteine is a competitive inhibitor for protein methylase II with K_i value of 1.6 × 10^?6m.     

Proteomics of the milk fat globule membrane from Camelus dromedarius

Camel milk has been widely characterized with regards to casein and whey proteins. However, in camelids, almost nothing is known about the milk fat globule membrane (MFGM), the membrane surrounding fat globules in milk. The purpose of this study was thus to identify MFGM proteins from Camelus dromedarius milk. Major MFGM proteins (namely, fatty acid synthase, xanthine oxidase, butyrophilin, lactadherin, and adipophilin) already evidenced in cow milk were identified in camel milk using MS. In addition, a 1D‐LC‐MS/MS approach led us to identify 322 functional groups of proteins associated with the camel MFGM. Dromedary MFGM proteins were then classified into functional categories using DAVID (the Database for Annotation, Visualization, and Integrated Discovery) bioinformatics resources. More than 50% of MFGM proteins from camel milk were found to be integral membrane proteins (mostly belonging to the plasma membrane), or proteins associated to the membrane. Enriched GO terms associated with MFGM proteins from camel milk were protein transport (p‐value = 1.73 × 10^?14), translation (p‐value = 1.08 × 10^?11), lipid biosynthetic process (p‐value = 6.72 × 10^?10), hexose metabolic process (p‐value = 1.89 × 10^?04), and actin cytoskeleton organization (p‐value = 2.72 × 10^?04). These findings will help to contribute to a better characterization of camel milk. Identified MFGM proteins from camel milk may also provide new insight into lipid droplet formation in the mammary epithelial cell.     

Risk Assessment for Natural Uranium in Subsurface Water of Punjab State,India

Traces of uranium were measured by laser fluorimeter in 235 subsurface water samples collected from four districts of Punjab state in India. The concentration of U in water samples ranged between <2–644 μg/L with a mean value of 73.1 μg/L. The radiological risk was observed to be in the range of 5.55 × 10^?6–1.78 × 10^?3 with a mean value of 2.03 × 10^?4, which is around 22% more than the maximum acceptable level (l.67 × 10^?4) as per guidelines of India's Atomic Energy Regulatory Board. The mean of chemical toxicity risk, expressed as life time average daily dose (LADD) was worked out to be 5.56 μg/kg/day with a range of 0.15–48 μg/kg/day by considering a bodyweight of 51.5 ± 8.5 kg, water ingestion rate of 4.05 L/d, and life expectancy of 63.7 yrs for an adult Indian reference man and compared with the reference dose (4.53 μg/kg/day). The average exposure level of U was comparatively high and the chemical toxicity was expected to be more. The mean of hazard quotient (LADD/ RfD) for all four districts was found to be greater than 1, indicating that groundwater may not be suitable for consumption from a chemical toxicity point of view.     

Hydrodynamic properties of mushroom tyrosinase

The hydrodynamic properties of mushroom tyrosinase were determined at pH 6.5 using a Sephadex G-200 column. From the comparison of its gel-filtration behaviour with those of standard proteins, the following parameters were calculated: MW (122 500 ± 1%), Stokes' radius (42.75 × 10^?8 cm²/sec), diffusion coefficient (5.048 × 10^?7 cm²/sec) and frictional ratio (1.26). These values suggest a globular conformation of this enzyme.     

Conformation of <Emphasis Type="Italic">Thermus thermophilus</Emphasis> ribosomal protein S1 in solution at different ionic strengths

Small-angle x-ray and neutron scattering were used to study the structure of the ribosomal protein S1 (61 kDa) from Thermus thermophilus in solution at low and moderate ionic strength (0 and 100 mM NaCl). The protein was found to be globular in both cases. Modeling of the S1 structure comprising six homologous domains on the basis of the NMR data for one domain showed that the best fit to scattering data was provided by compact domain packing. The calculated gyration radius was 28–29 Å, as typical of globular proteins about 60 kDa. The protein was prone to self-association, forming mainly dimers and trimers at moderate ionic strength and higher compact associates at low ionic strength. Neutron scattering assays in heavy water at 100 mM NaCl revealed markedly elongated associates. The translational diffusion coefficient calculated for S1 at 100 mM NaCl from dynamic light scattering was markedly lower than the one expected for its globular monomer (D _20,w = (2.7 ± 0.1)·10^?7 versus (5.8–6.0)·10^?7 cm² s^?1), confirming protein association under equilibrium conditions.     

Trihalomethanes in desalinated water: Human exposure and risk analysis

Desalinated seawater is used to satisfy domestic water demands in many countries. The treated freshwater is blended with desalinated water to increase the water supply. The desalinated and blended water contains disinfection byproducts (DBPs), some of which may induce cancer risk to human. In this study, concentrations of trihalomethanes (THMs) in desalinated and blended water in Saudi Arabia were investigated, and human exposure and risk were predicted. The intakes of THMs (chloroform, bromodichloromethane, dibromochloromethane, and bromoform) were predicted to be 8.38 × 10^?5, 7.57 × 10^?5, 2.54 × 10^?5, and 4.32 × 10^?4 mg/kg-d, respectively. The overall cancer risk and hazard index were estimated to be 1.78 × 10^?5 (range: 7.40 × 10^?7–9.26 × 10^?5) and 3.49 × 10^?2 (range: 1.20 × 10^?3–2.34 × 10^?1), respectively. The probabilities of cancer risk exceeding the risk levels of 1 × 10^?6, 1 × 10^?5, and 5.0 × 10^?5 were 1.0, 0.775, and 0.012, respectively. The loss of disability adjusted life years (DALYs) was predicted to be 25.1 per year while the cancer risk represented 8.48 × 10^?7 DALY per person per year. The financial burden from such risk was estimated to be US$ 2.72 (range: US$ 2.52–2.91) million per year. The findings may assist in better understanding and reducing cancer risk from DBPs in desalinated and blended water.     

Refolding of Npro fusion proteins

The autoprotease N^pro significantly enhances expression of fused peptides and proteins and drives the formation of inclusion bodies during protein expression. Upon refolding, the autoprotease becomes active and cleaves itself specifically at its own C‐terminus releasing the target protein with its authentic N‐terminus. N^pro wild‐type and its mutant EDDIE, respectively, were fused N‐terminally to the model proteins green fluorescent protein, staphylococcus Protein A domain D, inhibitory peptide of senescence‐evasion‐factor, and the short 16 amino acid peptide pep6His. In comparison with the N^pro wild‐type, the tailored mutant EDDIE displayed an increased rate constant for refolding and cleavage from 1.3 × 10^?4 s^?1 to 3.5 × 10^?4 s^?1, and allowed a 15‐fold higher protein concentration of 1.1 mg/mL when studying pep6His as a fusion partner. For green fluorescent protein, the rate constant was increased from 2.4 × 10^?5 s^?1 to 1.1 × 10^?4 s^?1 when fused to EDDIE. When fused to small target peptides, refolding and cleavage yields were independent of initial protein concentration, even at high concentrations of 3.9 mg/mL, although cleavage rates were strongly influenced by the fusion partner. This behavior differed from conventional 1st order refolding kinetics, where yield strongly depends on initial protein concentration due to an aggregation reaction of higher order. Refolding and cleavage of EDDIE fusion proteins follow a monomolecular reaction for the autoproteolytic cleavage over a wide concentration range. At high protein concentrations, deviations from the model assumptions were observed and thus smaller rate constants were required to approximate the data. Biotechnol. Bioeng. 2009; 104: 774–784 © 2009 Wiley Periodicals, Inc.     

Catalytic resonance scattering spectral determination of ultratrace horseradish peroxidase using rhodamine S

A highly sensitive and selective resonance scattering spectral assay was proposed for the determination of horseradish peroxidase (HRP), based on its catalytic effect on the H₂O₂ oxidation of KI to form I₃^?. The I₃^? combined respectively with rhodamine (Rh) dye such as rhodamine S (RhS), rhodamine 6G (Rh6G), rhodamine B (RhB) and butyl‐rhodamine B (b‐RhB), to form association particles (Rh‐I₃)_n. The four Rh systems all exhibit a stronger resonance scattering (RS) peak at 424 nm. For the RhS, Rh6G, RhB and b‐RhB systems, HRP concentration in the range of 3.2 × 10^?12 to 4.8 × 10^?9, 2 × 10^?11 to 3.2 × 10^?9, 1.6 × 10^?11 to 3.2 × 10^?9 and 1.6 × 10^?11 to 4 × 10^?9 g/mL was linear to its RS intensity at 424 nm, with a detection limit of 2.2 × 10^?12, 2.5 × 10^?12, 4.4 × 10^?12 and 2.6 × 10^?12 g/mL, respectively. This RhS system was most sensitive and stable, and was applied for the determination of HRP in the hepatitis B surface antibody labeling HRP and water samples, with satisfactory results. Copyright © 2009 John Wiley & Sons, Ltd.     

Resonance light‐scattering enhancement effect of the protein–Y3+–TTA–SLS system and its analytical application

In this paper, a sensitive resonance light scattering (RLS) method for the determination of protein is reported. In the Tris–HCl (pH 7.50) buffer, protein enhanced the RLS intensity of the Y³⁺–2‐thenoyltrifluoroacetone (TTA)–sodium dodecyl sulphate (SLS) system. The enhanced RLS intensities were in proportion to the concentrations of proteins in the range 8.0 × 10^?9–1.0 × 10^?5 g/mL for BSA, 1.0 × 10^–8–1.0 × 10^?5 g/mL for HSA and 1.0 × 10^–8–1.0 × 10^?6 g/mL for EA, and their detection limits were 5.0, 5.4 and 6.7 ng/mL, respectively. Actual samples were satisfactorily determined. The interaction mechanism was also studied. Copyright © 2008 John Wiley & Sons, Ltd.     

A novel microtechnique for the measurement of acoustic properties of lipids

Application of a new microtechnique is described for the derivation of acoustic properties (ultrasonic velocity, adiabatic compressibility and acoustic impedance) of lipids. The technique utilizes very small volumes (4 × 10^?3 ?4 × 10^?6 ml) of lipids and thus overcomes the requirement for large volumes inherent in the use of conventional velocimeters. The use of the microtechnique allows acoustic properties to be included among the variety of other physical properties routinely measured in the characterization of lipids, including those isolated in small amounts from complex biological mixtures.     

Quantitative and qualitative study of the bacterial flora of farmed freshwater prawn (Macrobrachium rosenbergii) larvae

Quantitative and qualitative studies of the bacterial flora of farmed freshwater prawn (Macrobrachium rosenbergii) larvae in Saudi Arabia were performed, and isolates identified where possible. Physico‐chemical characteristics, bacterial counts, and the nature of the bacterial flora of larvae rearing tank water, sediment, tank wall surfaces, larval surface, supplied water, and feed were investigated. Bacterial counts ranged from 2.1 ± 1.3 × 10⁵ to 2.2 ± 0.8 × 10⁷ colony forming units (CFU) ml^?1 in tank water; 4.4 ± 0.9 × 10⁷ to 8.3 ± 1.7 ×10⁹ CFU g^?1 in tank sediment; 8.6 ± 1.0 × 10² to 9.8 ±0.7 × 10⁴ CFU cm^?2 on the tank wall surface; 1.3 ± 1.1 × 10⁴ to 7.7 ± 1.6 × 10⁶ CFU per larva surface, 7.9 ± 1.2 × 10⁵ to 5.0 ± 1.5 × 10⁷ CFU g^?1 in washed larval tissue slurries, 9.1 ± 0.7 × 10³ CFU ml^?1 in supplied water, and 2.4 ± 1.9 ×10¹⁰ CFU g^?1 in mixed feed. Fourteen bacterial genera were identified, including Chryseomonas sp., Vibrio spp., Cellulomonas sp., Aeromonas hydrophila, and Pasteurella sp. The tank water and sediment had similar bacteria to those on the prawn larvae. Chryseomonas sp., Cellulomonas sp. and Vibrio sp. were the most dominant species (prevalence >10%) in tank water; Chryseomonas sp., Pseudomonas alcaligenes and Shewanella putrefaciens in the sediment; Ps. alcaligenes and Cellulomonas sp. on the tank wall surface; Chryseomonas sp., and Cellulomonas sp. on the larval surface; and Chryseomonas sp., Vibrio vulnificus, Sh. putrefaciens and V. alginolyticus in the washed larval tissue slurries (prevalence 10%). Pseudomonas alcaligenes, Moraxella sp., Serratia liquefaciens, Gordona sp. and Burkholderia glumae were absent in larvae but identified in the culture water, tank sediment, and tank wall surface. Pseudomonas sp., Chryseomonas sp., Pasteurella sp. and V. alginolyticus were the prevalent bacteria (>12%) in supplied water. The feed contained V. alginolyticus, A. hydrophila and Cellulomonas sp. as the dominant bacteria (>13%). In the culture water and larvae samples, 83% of the feed and supplied water bacteria were identified.     

Production of phenolic compounds in callus cultures of tea plant under the effect of 2,4-D and NAA

The effect of hormone-like compounds at different concentrations: 2,4-D (2 × 10^?6; 2 × 10^?5; and 2 × 10^?4M) and 1-NAA (2 × 10^?7; 2 × 10^?6; 2 × 10^?5; 4 × 10^?5, and 6 × 10^?5 M) on the growth and production of phenolic compounds, including flavans and lignin, was investigated in callus culture of tea plant (Camellia sinensis L., a highly productive strain IFR ChS-2). The growth of the culture was vigorous, and production of phenolic compounds therein was efficient in the medium containing 2 × 10^?5 M 2,4-D. Substitution of 1-NAA for 2,4-D in all the cases decelerated the growth of the culture. These changes were more pronounced when 2 × 10^?7 and 2 × 10^?6 M 1-NAA was used; in this case, biomass accumulation decreased by 1.5–2.0 times as compared with control material growing on the medium with 2 × 10^?5 M 2,4-D. In the presence of 1-NAA, the content of total soluble phenolic compounds and flavans in the calli rose by 30% on the average as compared with control material. Accumulation of lignin remained essentially the same. Therefore, the replacement of 2,4-D with 1-NAA in the nutrient medium used for the growing of highly productive strain of tea plant callus did not induce considerable changes in its ability to produce phenolic compounds.     

Translational diffusion in the plasma membrane of sea urchin eggs

Translational diffusion in the plasma membrane of individual egg cells from the sea urchin species Paracentrotus lividus has been studied by fluorescence microphotolysis (FM). In order to probe the lipid phase of the membrane, procedures have been worked out by which the fluorescent analog 3,3′-dioctadecyl-oxatricarbocyanine (C₁₈diO) can be incorporated into the membrane. In the unfertilized egg a fraction R = 0.9 of C₁₈diO was mobile having an apparent diffusion coefficient of D = 6.0 × 10^?9 cm² sec^?1. Fifteen to twenty-five minutes after fertilization R and D were reduced to 0.8 and 2.7 × 10^?9 cm² sec^?1, respectively. In order to study diffusion of membrane proteins, procedures have been worked out by which the cell surface can be labeled with fluorescein-isothiocyanate (FITC). FITC binds to both the plasma membrane and the vitelline layer. Together with the vitelline layer two-thirds of the FITC-fluorescence could be removed from the egg surface. Gel electropherograms of isolated egg cortices showed various protein bands; however, only two of the protein bands were labeled with FITC. In the unfertilized egg a fraction R = 0.9 of the FITC-labeled membrane proteins was mobile having an apparent diffusion coefficient of D = 35 × 10^?11 cm² sem^?1. Fiteen to twenty-five minutes after fertilization R and D were reduced to 0.8 and 7.0 × 10^?11 cm² sec^?1, respectively. FITC-labeled proteins of the fertilization envelope were immobile. Our studies have shown (i) that the egg surface can be fluorescently labeled without blocking fertilization and early development, (ii) that the plasma membrane of unfertilized eggs is a fluid environment permitting a rapid movement of lipids and proteins, and (iii) that after fertilization a substantial degree of lipid and protein mobility is maintained.     

Physical studies on proteins L3 and L24 from the 50 S subunit of the Escherichia coli ribosome.

Proteins L3 and L24, purified by a nondenaturing method from the 50 S ribosomal subunit of Escherichia coli A19, have been characterized. Both proteins were studied under conditions which resemble those used for reconstitution experiments. They were soluble at approximately 2–3 mg/ml and showed little or no aggregation. These proteins have s⁰_20,w values of 2.0 and 1.5 S, and D_20,w values of 7.6 × 10^?7 and 11.0 × 10^?7 cm² s^?1. Partial specific volumes at 20 °C are 0.730 and 0.740 ml g^?1 for the two proteins. The respective molecular weights determined by sedimentation equilibrium are 24,500 and 12,000. The intrinsic viscosity values for the two proteins are 6.0 and 4.0 ml g^?1. From these hydrodynamic parameters an elongated shape for L3 and a globular shape for L24 have been inferred.