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M K Jain

Publications and source records attributed to M K Jain.

At least 73 records · Page 4Linked to original sources

Effect of skin electrode location on radiofrequency ablation lesions: an in vivo and a three-dimensional finite element study.

INTRODUCTION OBJECTIVES: To assess the effect of skin electrode location on radiofrequency (RF) ablation lesion dimensions and energy requirements. BACKGROUND: Little is known about the effects of skin electrode location on RF ablation lesion dimensions and efficiency. METHODS AND RESULTS: Temperature-controlled ablation at 60 degrees C for 60 seconds was performed in six sheep. Paired lesions were created in the lateral, anterior, posterior, and septal walls of both the ventricles. For group 1 lesions, the skin electrode was positioned directly opposite the catheter tip (optimal). For group 2 lesions, we used either the standard posterior location or an anterior location if the posterior skin electrode location was used for group 1. Group 1 lesions were 5.8+/-0.8 mm deep and 9.3+/-1.9 mm wide, compared with 4.6+/-1.0 mm deep and 7.7+/-1.9 mm wide group 2 lesions (P < or = 0.001). Group 1 lesion dimensions also had less variability. A finite element model was used to simulate temperature-controlled ablation and to study the effect of skin electrode locations on lesion dimensions, ablation efficiency, and blood heating. The optimal location was 1.6 times more efficient, and the volume of blood heated to > or = 90 degrees C was 0.005 mm3 for optimal versus 2.2 mm3 for the nonoptimal location. CONCLUSION: Optimal skin electrode placement: (1) creates deeper and larger lesions; (2) reduces lesion size variability; and (3) decreases blood heating.

Animals↗

Role of TGF-beta in vascular development and vascular reactivity.

Transforming growth factor-beta (TGF-beta) is the prototypic member of a large family of structurally related proteins. Three vertebrate TGF-beta isoforms have been identified and termed TGF-beta1, TGF-beta2, and TGF-beta3, respectively. In addition, two receptors of the serine/threonine kinase family termed type I and II have also been identified. In this review, we focused our attention on the effects of TGF-beta on vascular development and vascular reactivity. The critical role of the TGF-beta1 and the TGF-beta type II receptor in blood vessel formation in the yolk sac has been demonstrated by gene deletion experiments. Recent investigations have also shown that isoforms of TGF-beta play a critical role in smooth muscle cell differentiation. And, finally, a role for TGF-beta1 in the regulation of vascular tone and reactivity has been suggested by studies demonstrating that TGF-beta1 can inhibit the production of potent vasodilators (such as nitric oxide) and stimulate the production of potent vasoconstrictors (such as endothelin). Taken together, these studies suggest that TGF-beta plays a critical role in blood vessel development and vascular function.

Animals↗

Thermodynamic and kinetic basis of interfacial activation: resolution of binding and allosteric effects on pancreatic phospholipase A2 at zwitterionic interfaces.

A general kinetic model for catalysis by interfacial enzymes is developed. It couples the Michaelis-Menten catalytic turnover cycle at the interface with that in the aqueous phase through the distribution equilibria between the interface and the surrounding aqueous phase. Analysis under two limiting conditions fully describes the steady-state kinetics of hydrolysis and resolves the allosteric effects from apparent modes of interfacial activation in terms of the primary rate and equilibrium parameters for pig pancreatic phospholipase A2 (PLA2). One limit is observed in dispersions of anionic phospholipid vesicles, in which intervesicle exchange of enzyme, substrate, and hydrolysis products is absent and reaction occurs only on vesicles containing enzyme. A complete analysis at this highly processive limit, called kinetics in the scooting mode, has been published [Berg et al. (1991) Biochemistry 30, 7283]. Here is reported the analysis in the other limit, PLA2-catalyzed hydrolysis of zwitterionic micelles of short-chain phosphatidylcholines, at which substrate and products are in rapid exchange. Hydrolysis occurs either in bulk aqueous solution with phospholipid monomers or at the micellar interface. Above the critical micelle concentration (cmc), the hydrolysis rate shows a hyperbolic dependence on the bulk substrate concentration present as micelles. This dependence, characterized by the fitting parameters KMapp and VMapp, is analyzed in terms of the primary rate and equilibrium constants. The kinetic analysis is based on the assumption that the microscopic steady-state condition is satisfied because substrate replenishment in the micro-environment of the enzyme is fast relative to the catalytic turnover time. Added NaCl and anionic interface increase the hydrolysis rate in zwitterionic micelles dramatically. The overall interfacial rate enhancement is attributed to three factors: (a) promotion of PLA2 binding by net anionic charge of the interface, (b) enhancement of substrate affinity of PLA2 at the interface (Ks* allostery), and (c) stimulation of the rate-limiting chemical step (kcat* allostery).

Allosteric Regulation↗

Crystal structure of the complex of bovine pancreatic phospholipase A2 with the inhibitor 1-hexadecyl-3-(trifluoroethyl)-sn-glycero-2-phosphomethanol,.

The structure of recombinant bovine pancreatic phospholipase A2 (PLA2) complexed with the competitive inhibitor 1-hexadecyl-3-(trifluoroethyl)-sn-glycero -2-phosphomethanol (hereafter MJ33), a phospholipid analogue without the sn-3 phosphodiester group, has been determined. The crystals are trigonal, space group P3121, a = b = 46.36 A and c = 102.56 A, and isomorphous to the recombinant PLA2 with one molecule in the asymmetric unit. The structure was refined using 8082 reflections between 8.0 and 1.91 A resolution to a final R-value of 18.4% [Rfree = 28.0%]. The model includes 957 protein atoms, 86 water molecules, one calcium ion, and 26 non-hydrogen atoms of the inhibitor MJ33. The overall tertiary fold of the complex is very similar to that of the inhibitor-free recombinant PLA2 with a root mean square deviation of 0.32 A for all the backbone atoms. The electron density of the surface loop residues 62-66 is clear and ordered, unlike the other trigonal bovine PLA2 structures done to date. This structural change could be responsible for the interfacial allosteric activation, which thermodynamically relates the enhanced binding of the substrate mimic to the active site of the enzyme. MJ33 is tightly bound in the active-site cleft, dislodging the equatorial coordinated calcium water (W5), the putative catalytic water W6, and the neighboring water W7. The axial coordinated calcium water is missing; thus the hexacoordinated calcium is a monocapped pentagonal pyramid. Although MJ33 is a sn-2 tetrahedral mimic, its phosphate binds to PLA2 differently from the sn-2 phosphonate analogue of phospholipids, another tetrahedral mimic. The knowledge of the active-site geometry of MJ33 would be useful in the design of more useful therapeutic agents for PLA2.

Animals↗

Gossypol modification of Ala-1 of secreted phospholipase A2: a probe for the kinetic effects of sulfate glycoconjugates.

Gossypol is shown to covalently modify secreted phospholipase A2 (PLA2) in the aqueous phase, but not at the interface. A rapid initial noncovalent binding of gossypol is followed by a slow covalent modification of the alpha-amino group of Ala-1 by stoichiometric amounts of gossypol. The rate of modification increases in the presence of calcium, but occupancy of the substrate binding site does not alter the rate. Pancreatic PLA2 is modified at the alpha-amino group of the N terminus to form a Schiff base, which can be stabilized by reduction with borohydride. Residual activity of the gossypol-modified PLA2 from several different sources is about 10%, indicative of impaired catalytic turnover. The half-time for the inactivation is about 10 min, and it is more than 100-fold longer for PLA2 at the interface. Gossypol promotes binding of PLA2 to the interface, and the binding of PLA2 to the interface promotes only the noncovalent binding of gossypol, but not the covalent modification. Gossypol, in conjunction with spectroscopic and kinetic protocols, is used to characterize the kinetic effects of sulfated glycoconjugates, heparin and artery wall proteoglycans, with human inflammatory and pancreatic PLA2.1 The conjugates do not interfere with the binding of PLA2 to the interface or with the catalytic cycle at the interface. The conjugates do not influence the kinetics of modification of PLA2 by gossypol in the aqueous phase, and the enzyme at the interface is not modified in the presence of the conjugates. The conjugates bind to PLA2 at the interface with only a modest effect on the interfacial catalytic turnover without dislodging the bound enzyme. Complex kinetic effects induced by the conjugates are shown to be due to sequestration of PLA2 in the aqueous phase as a high-molecular mass complex, which dissociates with added NaCl.

Alanine↗

The polymyositis-scleroderma autoantigen interacts with the helix-loop-helix proteins E12 and E47.

The basic helix-loop-helix (bHLH) transcription factors E12 and E47 regulate cellular differentiation and proliferation in diverse cell types. While looking for proteins that bind to E12 and E47 by the yeast interaction trap, we isolated the rat (r) homologue of the human (h) polymyositis-scleroderma autoantigen (PM-Scl), which has been localized to the granular layer of the nucleolus and to distinct nucleocytoplasmic foci. The rPM-Scl and hPM-Scl homologues are 96% similar and 91% identical. We found that rPM-Scl mRNA expression was regulated by growth factor stimulation in cultured rat aortic smooth muscle cells. rPM-Scl bound to E12 and E47 but not to Id3, Gax, Myb, OCT-1, or Max. The C terminus of rPM-Scl (amino acids 283-353) interacted specifically with a 54-amino acid domain in E12 that is distinct from the bHLH domain. Finally, cotransfection of rPM-Scl and E47 specifically increased the promoter activity of a luciferase reporter construct containing an E box and did not affect the basal activity of the reporter construct. rPM-Scl appears to be a novel non-HLH-interacting partner of E12/E47 that regulates E2A protein transcription.

Amino Acid Sequence↗

Use of an imperfect neutral diluent and outer vesicle layer scooting mode hydrolysis to analyze the interfacial kinetics, inhibition, and substrate preferences of bee venom phospholipase A2.

Interfacial catalytic constants for bee venom phospholipase A2 (bvPLA2) have been obtained for its action on vesicles of the anionic phospholipid 1,2-dimyristoylphosphatidylmethanol (DMPM) in the highly processive scooting mode. Spectroscopic measurements which directly measure transbilayer movement of membrane components show that this exchange does not occur in anionic vesicles that have undergone complete bvPLA2-catalyzed hydrolysis of all phospholipids in the outer vesicle monolayer. 3-Hexadecyl-sn-glycero-1-phosphocholine (D-LPC) is an adequate neutral diluent for bvPLA2, which is defined as an amphiphile that forms an aggregate to which enzyme binds but neutral diluent molecules bind weakly in the enzyme's active site. D-LPC has weak affinity for the active site of bvPLA2, and theory and protocols are developed that allow its use to determine equilibrium dissociation constants for competing active site ligands. Some of the properties of bvPLA2 are shared by other 14 kDa PLA2s. (1) Ca2+ is required for binding of ligands to the active site but not for the binding of enzyme to the interface. (2) bvPLA2 does not significantly discriminate between phospholipids with different polar head groups or acyl chains. (3) bvPLA2 does not bind to phosphatidylcholine vesicles, and binding occurs if anionic amphiphiles are present in the vesicle. Novel features of bvPLA2 include the following: (1) Neutral diluents for other 14 kDa phospholipases A2 are not neutral diluents for bvPLA2. (2) Saturation of the active site with a variety of different ligands does not completely prevent histidine alkylation by 2-bromo-4'-nitroacetophenone, and Ca2+ binding does not change the rate of histidine alkylation. Finally, the carbohydrate portion of bvPLA2 does not alter the interfacial catalytic properties of the enzyme. Kinetic analysis of bvPLA2 in the scooting mode together with previous studies with other 14 kDa PLA2s provides a paradigm for the quantitative analysis of interfacial catalysis.

Acetophenones↗

Synergism between mellitin and phospholipase A2 from bee venom: apparent activation by intervesicle exchange of phospholipids.

Mellitin, a cationic amphiphilic peptide, has an apparent activating effect on interfacial catalysis by phospholipase A2 (PLA2) of bee venom on zwitterionic vesicles of 1-palmitoyl-2-oleoylglycero-sn-3-phosphocholine (POPC) and on anionic vesicles of 1,2-dimyristoylglycero-sn-3-phosphomethanol (DMPM), as well as on covesicles of POPC/DMPM (3:7). On the other hand, mellitin-induced increase in the rate of pig pancreatic PLA2 is seen only on anionic vesicles. Interfacial kinetic protocols and spectroscopic methods show that the activation is due to enhanced substrate replenishment resulting from intervesicle exchange of zwitterionic or anionic phospholipids through vesicle-vesicle contacts established by mellitin. It is shown that as the hydrolysis on POPC vesicles progresses, due to a high propensity of bee PLA2 for binding to the product containing zwitterionic vesicles, most of the enzyme in the reaction mixture is trapped on few vesicles that are initially hydrolyzed, and thus reaction ceases. Under these conditions, mellitin promotes substrate replenishment by direct exchange of the products of hydrolysis from the enzyme-containing vesicles with the substrate present in excess vesicles which have not been hydrolyzed. Pig PLA2 has poor affinity for POPC vesicles, and the affinity is only modestly higher in the presence of low mole fractions of the products of hydrolysis; therefore, the enzyme is not trapped on those vesicles. Biophysical studies confirm that the phospholipid exchange occurs through stable intervesicle contacts formed by low mole fractions of mellitin, without transbilayer movement of phospholipids or fusion of vesicles. At high mole fraction (> 1.5%) mellitin induces leakage in POPC vesicles and does not form additional contacts. In POPC/DMPM vesicles, the contacts are formed even at high mole fractions of mellitin. Changes in intrinsic tryptophan fluorescence of mellitin indicate that bound mellitin exists in at least two different functional forms depending on the lipid composition and on the lipid:peptide ratio. A model is proposed to accommodate amphiphilic mellitin as a transmembrane channel or an intervesicle contact.

Acrylamide↗

Phospholipase A2 engineering. Structural and functional roles of the highly conserved active site residue aspartate-99.

The aspartate-99 of secreted phospholipase A2 (PLA2) has been proposed to be critical for the catalytic mechanism and interfacial activation of PLA2. Aspartate-99 connects the catalytic machinery (including the catalytic diad, the putative catalytic waters W5 and W6, and the calcium cofactor) to the hydrogen-bonding network. The latter involves Y52, Y73, the structural water, and the N-terminal region putatively required for the interfacial activation. A triple mutant of bovine pancreatic PLA2 with substitutions aspartate plus adjacent tyrosine residues (Y52,73F/D99N) was constructed, its X-ray structure was determined, and kinetic characteristics were analyzed. The kinetic properties of the D99N mutant constructed previously were also further analyzed. The X-ray structure of the Y52,73F/D99N mutant indicated a substantial disruption of the hydrogen-bonding network including the loss of the structural water similar to that seen in the structure of the D99N mutant published previously [Kumar, A., Sekharudu, Y. C., Ramakrishnan, B., Dupureur, C. M., Zhu, H., Tsai, M.-D., & Sundaralingam, M. (1994) Protein Sci. 3, 2082-2088]. Kinetic analysis demonstrated that these mutants possessed considerable catalytic activity with a k(cat) value of about 5% compared to WT. The values of the interfacial Michaelis constant were also little perturbed (ca. 4-fold lower for D99N and marginally higher for Y52,73F/D99N). The results taken together suggest that the hydrogen-bonding network is not critically important for interfacial activation. Instead, it is the chemical step that is perturbed, though only modestly, in the mutants.

Amino Acid Sequence↗

Salt-triggered intermembrane exchange of phospholipids and hemifusion by myelin basic protein.

Intervesicle phospholipid exchange through molecular contacts induced by the C1 molecular species of myelin basic protein (MBP) are characterized by using methods that amplify the effect of MBP-membrane interaction. The effect of salt concentration (KCl) on the vesicle-vesicle interaction of anionic sonicated covesicles of 30% 1-palmitoyl-2-oleoylglycero-sn-3-phosphocholine and 70% 1,2-dimyristoylglycero-sn-3-phosphomethanol (POPC/DMPM) by MBP is dissected by a combination of protocols into individual steps: aggregation of vesicles, apposition and contact formation, and hemifusion. Scattering and resonance energy transfer measurements reveal that, in the absence of KCl, MBP promotes rapid aggregation of the vesicles without lipid mixing. At >40 mM KCl, the extent of aggregation is larger and time-dependent. Fluorescence dequenching due to dilution of labeled phospholipids indicates that on a somewhat slower time scale, hemifusion of vesicles is triggered by salt, with mixing of the outer monolayer lipids but without flip-flop of phospholipids and without mixing or leakage of the aqueous contents. The exchange and hemifusion are seen with anionic vesicles; the effect of the structure of phospholipid, composition of vesicles, and the protein/lipid ratio is primarily on the kinetics of these and other competing processes. Thus, at 0.022 mol % of MBP and less than 100 mM KCl, it is possible to uncouple three sequential steps: (1) aggregation of vesicles by MBP; (2) apposition of bilayers and selective lipid exchange through vesicle-vesicle contacts established by MBP, i.e., anionic and zwitterionic phospholipids exchange, but cationic probes are excluded; and (3) hemifusion and lipid mixing of contacting monolayers of vesicles.

Anions↗

A case-control analysis of risk factors in HIV transmission in South India.

A case-control study was done among patients attending our clinic for sexually transmitted diseases in South India to assess risk factors for human immunodeficiency virus (HIV) infection. Of 5,876 patients tested, 105 (1.79%) were HIV antibody positive (87 men, 18 women) by enzyme-linked immunosorbent assay and Western blot. They were compared with an equal number of age- and sex-matched patients without HIV antibody. Risk factors significant in the crude odds ratio analysis were occupation (truck drivers and truck cleaners), age at first exposure, and sexual contact with commercial sex workers. In the logistic regression analysis, only a history of past genital ulcer was a significant risk factor. Other important findings of this study were that (a) the spread of HIV to women is mostly from their infected husbands and (b) regular condom use was reported by less than 8% of patients and controls. Obviously, the current methods of education of the population are far from adequate.

Adult↗

Identification of a human cDNA clone for lysosomal type Ca2+-independent phospholipase A2 and properties of the expressed protein.

A Ca2+-independent phospholipase A2 (PLA2) maximally active at pH 4 and specifically inhibited by the transition-state analogue 1-hexadecyl-3-trifluoroethylglycero-sn-2-phosphomethanol (MJ33) was isolated from rat lungs. The sequence for three internal peptides (35 amino acids) was used to identify a 1653-base pair cDNA clone (HA0683) from a human myeloblast cell line. The deduced protein sequence of 224 amino acids contained a putative motif (GXSXG) for the catalytic site of a serine hydrolase, but showed no significant homology to known phospholipases. Translation of mRNA produced from this clone in both a wheat germ system and Xenopus oocytes showed expression of PLA2 activity with properties similar to the rat lung enzyme. Apparent kinetic constants for PLA2 with dipalmitoylphosphatidylcholine as substrate were Km = 0.25 mM and Vmax = 1.89 nmol/h. Activity with alkyl ether phosphatidylcholine as substrate was decreased significantly compared with diacylphosphatidylcholine. Significant lysophospholipase, phospholipase A1, or 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine acetylhydrolase activity was not observed. Enzyme activity was insensitive to p-bromophenacyl bromide, bromoenol lactone, trifluoromethylarachidonoyl ketone, mercaptoethanol, and ATP, but was inhibited by MJ33 and diethyl p-nitrophenyl phosphate, a serine protease inhibitor. SDS-polyacrylamide gel electrophoresis with autoradiography of the translated [35S]methionine-labeled protein confirmed a molecular mass of 25.8 kDa, in good agreement with the enzyme isolated from rat lung. By Northern blot analysis, mRNA corresponding to this clone was present in both rat lung and isolated rat granular pneumocytes. These results represent the first molecular cloning of a cDNA for the lysosomal type Ca2+-independent phospholipase A2 group of enzymes.

Amino Acid Sequence↗

Effect of surgical experience on results of esophagectomy for esophageal carcinoma.

BACKGROUND: Esophagectomy for esophageal cancer is associated with substantial operative morbidity and mortality. The effect of surgical experience on results of esophagectomy has received little attention in the medical literature. METHODS: A retrospective review of esophagectomies for cancer was done. RESULTS: Seventy-four patients underwent esophagectomy by 20 different surgeons. Three surgeons performed 6 or more esophagectomies per year ("frequent" surgeons), whereas the other 17 surgeons performed 5 or fewer esophagectomies per year ("occasional" surgeons). Forty-two patients were operated on by frequent surgeons. There were 3 (7%) anastomotic leaks and no deaths. In 32 patients operated on by occasional surgeons, there were 7 (22%) anastomotic leaks and 7 (22%) operative deaths. The anastomotic leak rates were not significantly different (P < .07), but frequent surgeons had a significantly lower operative mortality (P < .0014). CONCLUSIONS: Esophagectomy for esophageal cancer should be performed by experienced esophageal surgeons with sufficient yearly volume of procedures to maintain competence.

Esophageal Neoplasms↗

Environmental and physiological factors affecting the succinate product ratio during carbohydrate fermentation by Actinobacillus sp. 130Z.

Actinobacillus sp. 130Z fermented glucose to the major products succinate, acetate, and formate. Ethanol was formed as a minor fermentation product. Under CO2-limiting conditions, less succinate and more ethanol were formed. The fermentation product ratio remained constant at pH values from 6.0 to 7.4. More succinate was produced when hydrogen was present in the gas phase. Actinobacillus sp. 130Z grew at the expense of fumarate and l-malate reduction, with hydrogen as an electron donor. Other substrates such as more-reduced carbohydrates (e.g., d-sorbitol) resulted in higher succinate and/or ethanol production. Actinobacillus sp. 130Z contained the key enzymes involved in the Embden-Meyerhof-Parnas and the pentose-phosphate pathways and contained high levels of phosphoenolpyruvate (PEP) carboxykinase, malate dehydrogenase, fumarase, fumarate reductase, pyruvate kinase, pyruvate formate-lyase, phosphotransacetylase, acetate kinase, malic enzyme, and oxaloacetate decarboxylase. The levels of PEP carboxykinase, malate dehydrogenase, and fumarase were significantly higher in Actinobacillus sp. 130Z than in Escherichia coli K-12 and accounted for the differences in succinate production. Key enzymes in end product formation in Actinobacillus sp. 130Z were regulated by the energy substrates.

Actinobacillus↗

Leukotrienes in acetylcholine-induced contraction of esophageal circular smooth muscle in experimental esophagitis.

BACKGROUND & AIMS: Phospholipase A2 (PLA2) participates in acetylcholine (ACh)-induced contraction of esophageal circular smooth muscle. Because PLA2, arachidonic acid, and its metabolites are involved in inflammatory responses, their role after induction of experimental esophagitis was examined. METHODS: Experiments were performed in esophageal smooth muscle cells (ESO) isolated by enzymatic digestion from the circular layer of normal and esophagitis animals. Content of peptidoleukotrienes (leukotriene [LT] C4, LTD4, and LTE4) was measured in esophageal circular muscle tissue. RESULTS: The cytosolic PLA2 antagonist trifluoromethyl ketone analogue of arachidonic acid inhibited ACh-induced contraction of normal and esophagitis ESO. Inhibition by secreted PLA2 antagonists AM5 and MJ33 was significantly greater in esophagitis ESO. The lipoxygenase inhibitor nordihydro-guaiaretic acid and the LTD4 antagonist ICI 198,615 inhibited ACh-induced contraction of esophagitis but not of normal ESO. Secreted PLA2 and LTD4 contracted normal ESO more than esophagitis ESO. However, in esophagitis, ESO contraction was increased by threshold diacylglycerol concentration. Resting levels of LTs were greater in esophagitis than in normal circular esophageal muscle and increased in response to ACh in esophagitis but not in normal esophageal muscle. CONCLUSIONS: Esophagitis shifts the signal transduction pathway activated by ACh. Esophagitis increased the contribution of secreted PLA2 and of LTs to ACh-induced contraction.

Acetylcholine↗

Composition and role of extracellular polymers in methanogenic granules.

Methanobacterium formicicum and Methanosarcina mazeii are two prevalent species isolated from an anaerobic granular consortium grown on a fatty acid mixture. The extracellular polysaccharides (EPS) were extracted from Methanobacterium formicicum and Methanosarcina mazeii and from the methanogenic granules to examine their role in granular development. The EPS made up approximately 20 to 14% of the extracellular polymer extracted from the granules, Methanobacterium formicicum, and Methanosarcina mazeii. The EPS produced by Methanobacterium formicicum was composed mainly of rhamnose, mannose, galactose, glucose, and amino sugars, while that produced by Methanosarcina mazeii contained ribose, galactose, glucose, and glucosamine. The same sugars were also present in the EPS produced by the granules. These results indicate that the two methanogens, especially Methanobacterium formicicum, contributed significantly to the production of the extracellular polymer of the anaerobic granules. Growth temperature, substrates (formate and H(inf2)-CO(inf2)), and the key nutrients (nitrogen and phosphate concentrations) affected polymer production by Methanobacterium formicicum.

Journal Article↗