A fluorimetric method for the estimation of G+C mol% content in microorganisms by thermal denaturation temperature

2002 ◽  
Vol 4 (11) ◽  
pp. 770-773 ◽  
Author(s):  
J. M. Gonzalez ◽  
C. Saiz-Jimenez
Keyword(s):  
Thermal Denaturation ◽  
Denaturation Temperature ◽  
Fluorimetric Method ◽  
Thermal Denaturation Temperature

Mesophilic mutants of an obligate psychrophile, Micrococcus cryophilus

1969 ◽  
Vol 15 (10) ◽  
pp. 1145-1150 ◽  
Author(s):  
P-C. Tai ◽  
H. Jackson
Keyword(s):  
Growth Temperature ◽  
Metabolic Pathways ◽  
Thermal Denaturation ◽  
Deoxyribonucleic Acid ◽  
Elevated Temperatures ◽  
Maximum Growth ◽  
Maximal Growth ◽  
Denaturation Temperature ◽  
Maximum Growth Temperature ◽  
Thermal Denaturation Temperature

Several mutants with elevated maximal growth temperature (MGT) were developed from an obligate psychrophile, Micrococcus cryophilus ATCC 15174, by ultraviolet irradiation. Two of the mutants, T8 and M19, have the most similar characteristics to those of their parent. The mutants lost the ability to grow well at 0 °C and showed changes in metabolic pathways while acquiring the ability to grow at elevated temperatures. Heat resistance and deoxyribonucleic acid thermal denaturation temperature were shown to be unrelated to maximum growth temperature. The significance of the mutants is discussed.

Similar C-phycocyanins from two strains of thermotolerant cyanophyte Mastigocladus laminosus

1977 ◽  
Vol 23 (5) ◽  
pp. 510-517 ◽  
Author(s):  
Oranda H. W. Kao ◽  
Donald S. Berns
Keyword(s):  
Elevated Temperature ◽  
Thermal Denaturation ◽  
Ph Value ◽  
Blue Green Alga ◽  
Denaturation Temperature ◽  
Mastigocladus Laminosus ◽  
Thermal Denaturation Temperature ◽  
Temperature Ranges ◽  
Synechococcus Lividus ◽  
Immunologic Properties

C-phycocyanin from two strains of the thermotolerant blue-green alga, Mastigocladus laminosus (NZ-DB2-m and I-30-m), that grow within different temperature ranges have been characterized with respect to aggregation, immunologic properties, subunit composition, and thermodenaturation. The critical thermal-denaturation temperature for phycocyanin from both strains of M. laminosus phycocyanin is 60 °C which is higher than that for mesophilic phycocyanin. Immunodiffusion studies have shown that these two strains of M. laminosus exhibit no antigenic differences and are closely related to the mesophilic Plectonema calothricoides and the thermophilic Synechococcus lividus (strain 3). Neither phenol nor α-naphthol has any effect on phycocyanin aggregation in these two strains of M. laminosus. There is also no enhancement of formation of large aggregates at their elevated temperature of cultivation. Furthermore, the phycocyanin of both strains of M. laminosus does not demonstrate any large amount of 19S or higher aggregates at any pH value. These observations suggest that the mode of adaptation of M. laminosus phycocyanin to high temperature is different from that previously encountered. It is also important to note that phycocyanin is essentially unchanged whether it is extracted from the same strain, M. laminosus (NZ-DB2-m), grown at either 50° or 37 °C.

Effect of carboidiimide on thermal denaturation temperature of dentin collagen

2016 ◽  
Vol 32 (4) ◽  
pp. 492-498 ◽  
Author(s):  
Milena Cadenaro ◽  
Luca Fontanive ◽  
Chiara Ottavia Navarra ◽  
Pietro Gobbi ◽  
Annalisa Mazzoni ◽  
...  
Keyword(s):  
Thermal Denaturation ◽  
Denaturation Temperature ◽  
Thermal Denaturation Temperature ◽  
Dentin Collagen

Isolation and characterisation of acid- and pepsin-soluble collagen from the skin of Cervus korean TEMMINCK var. mantchuricus Swinhoe

2018 ◽  
Vol 58 (3) ◽  
pp. 585 ◽  
Author(s):  
Gaurav Lodhi ◽  
Yon-Suk Kim ◽  
Eun-Kyung Kim ◽  
Jin-Woo Hwang ◽  
Hyung-Sik Won ◽  
...  
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Thermal Denaturation ◽  
Peptide Hydrolysis ◽  
Denaturation Temperature ◽  
Soluble Collagen ◽  
Acid Soluble Collagen ◽  
Thermal Denaturation Temperature ◽  
Skin Collagen ◽  
Pepsin Soluble Collagen ◽  
Calf Skin

Acid-soluble collagen and pepsin-soluble collagen were extracted from the skin of deer, Cervus korean TEMMINCK var. mantchuricus Swinhoe. The two types of collagen were then characterised using sodium dodecyl sulfate–polyacrylamide gel electrophoresis, amino acid composition analysis, peptide hydrolysis patterns, thermal denaturation temperature, differential scanning calorimetry, Fourier transform infrared spectroscopy, and nuclear magnetic resonance imaging. The yield of pepsin-soluble collagen (9.62%) was greater than that of acid-soluble collagen (2.24%), but both types of collagen showed similar electrophoretic patterns with each other and with calf skin collagen. The peptide hydrolysis pattern results suggested that calf skin collagen and pepsin-soluble collagen from deer skin may be similar in terms of their primary structure. The thermal denaturation temperature of acid-soluble collagen and pepsin-soluble collagen were 36.67°C and 36.44°C, respectively, and their melting temperatures were 110°C and 120°C, respectively, which suggest high thermal stability. Fourier transform infrared showed a triple helical structure and nuclear magnetic resonance confirmed the presence of ‘hydration’ water. These results provide a basis for large-scale production and further application as alternatives to other mammalian collagens.

scholarly journals Rapid Photoinduced Single Cell Detachment from Gold Nanoparticle-Embedded Collagen Gels with Low Denaturation Temperature

Polymers ◽  
2020 ◽  
Vol 12 (1) ◽  
pp. 213
Author(s):  
Chie Kojima ◽  
Misaki Nishio ◽  
Yusuke Nakajima ◽  
Takeshi Kawano ◽  
Kenji Takatsuka ◽  
...  
Keyword(s):  
Single Cell ◽  
Gold Nanoparticle ◽  
Thermal Denaturation ◽  
Collagen Gel ◽  
Collagen Fibers ◽  
Photothermal Effect ◽  
Cell Detachment ◽  
Type I ◽  
Collagen Gels ◽  
Denaturation Temperature

Cell Separation is important in various biomedical fields. We have prepared gold nanoparticle (AuNP)-embedded collagen gels as a visible-light-responsive cell scaffold in which photoinduced single cell detachment occurs through local thermal denaturation of the collagen gel via the photothermal effect of AuNP. Physicochemical properties of collagen materials depend on the origin of the collagen and the presence of telopeptides. In this study, we prepared various AuNP-embedded collagen gels by using different collagen materials with and without the telopeptides to compare their thermal denaturation properties and photoinduced single cell detachment behaviors. Cellmatrix type I-C without telopeptides exhibited a lower denaturation temperature than Cellmatrix type I-A and Atelocell IAC, as examined by Fourier transform infrared (FTIR) spectroscopy, rheological analysis, and sol–gel transition observation. Three-dimensional (3D) laser microscopic imaging revealed that collagen fibers shrank in Cellmatrix type I-A upon heating, but collagen fibers disappeared in Cellmatrix type I-C upon heating. Cells cultured on the Cellmatrix type I-C-based AuNP-embedded collagen gel detached with shorter photoirradiation than on the Cellmatrix type I-A-based AuNP-embedded collagen gel, suggesting that collagen gels without telopeptides are suitable for a photoinduced single cell detachment system.

BOVINE SERUM ALBUMIN DENATURATION IN THE PRESENCE OF HOECHST 33258 AND METHYLENE BLUE

2020 ◽  
Vol 54 (3 (253)) ◽  
pp. 204-208
Author(s):  
P.O. Vardevanyan ◽  
M.S. Mikaelyan ◽  
N.H. Petrosyan
Keyword(s):  
Methylene Blue ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Thermal Denaturation ◽  
Native Structure ◽  
Hoechst 33258 ◽  
Denaturation Temperature

The interaction of Hoechst 33258 (H33258) and methylene blue (MB) compounds with bovine serum albumin (BSA) has been studied using the method of thermal denaturation. The obtained data showed that both ligands form complexes with BSA, moreover, MB binds to BSA stronger than H33258. Furthermore, H33258 destabilizes, while MB stabilizes the native structure of protein, leading to the decrease and increase of the denaturation temperature of BSA respectively.

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