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Copyright of Revista Brasileira de Medicina do Esporte is the property of Redprint Editora Ltda. and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Revista Brasileira de Medicina do Esporte is the property of Redprint Editora Ltda. and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

NAD + -dependent glyceraldehyde dehydrogenases usually had lower activity in the nonphosphorylated Entner–Doudoroff (nED) pathway. In the present study, a new NAD + -dependent glyceraldehyde dehydrogenase was engineered froml-lactaldehyde dehydrogenase ofE. coli(EC: 1.2.1.22). Through comparison of the sequence alignment and the active center model, we found that a residue N286 ofl-lactaldehyde dehydrogenase contributed an important structure role to substrate identification. By free energy calculation, three mutations (N286E, N286H, N286T) were chosen to investigate the change of substrate specificity of the enzyme. All mutants were able to oxidate glyceraldehyde. Especially, N286T showed the highest activity of 1.1U/mg, which was 5-fold higher than the reported NAD + -dependent glyceraldehyde dehydrogenases, and 70% activity was retained at 55 °C after an hour. Compared tol-lactaldehyde, N286T had a one-third lowerKmvalue to glyceraldehyde. Molecular structure ofl-lactaldehyde dehydrogenase fromE. coli. [ABSTRACT FROM PUBLISHER]

Although widely used in sports, the efficiency of cryotherapy in reducing muscle damage has been questioned. The present study investigated the acute effects of post-exercise cryotherapy on the expression of creatine phosphokinase (CPK) and lactate dehydrogenase (LDH), perceived pain, and muscle strength of the upper limbs in Brazilian jiu-jitsu competitors. Nine highly trained fighters were subjected to two 90-minute training sessions. After the first session, five random subjects were immersed in a pool with ice (5±1°C) for nineteen minutes, and the remaining participants were allocated to the control group. The treatments were reversed in the second session (cross-over design). Analysis of covariance with repeated measures was used to compare outcomes between the groups, and pre-test measures were used as covariates. Pearson's correlation was adopted to check the strength of the associations between variables. The results showed lower serum CPK concentrations (P<0.05) in the cryotherapy group (504.0±138.7 IU/L) compared to the pre-exercise (532.6 ± 67.9 IU/L) group, and a similar result was observed for LDH (517.4±190.3 vs. 601.8±75.7 IU/L). Cryotherapy resulted in lower (P<0.05) perceived pain (2.2 ± 1.6 vs. 4.2 ± 1.9) and body temperature (34.2±1.3°C vs. 36.3±0.7°C), and an attenuated loss of isometric strength (53.1±18.1 s vs. 42.9±14.5 s). Perceived pain was directly associated (P<0.05) with CPK (r=0.59) and LDH (r=0.475) levels. The results show that post-exercise cryotherapy resulted in lower serum CPK and LDH, hypoalgesia, and greater preservation of isometric strength endurance when compared to the control condition. [ABSTRACT FROM AUTHOR]

The article presents a study that describes the genetic engineering of Candida utilis yeast. The methods used were recombinant DNA techniques, molecular cloning, and breeding of yeast strains. The results show that the constructed strain has a high L-lactic acid productivity than the other genetically modified yeasts, and that the amino acid sequences of various yeast species and pyruvate decarboxylase (PDC) genes show that their carboxyl termini were conserved.

The article focuses on the study conducted in Japan regarding the importance of Cathepsin L in the lysosomal degradation of L-lactate dehydrogenase (LDH). The authors discuss the inactivation and degradation of LDH inhibited by low level cystatin and general cysteine proteinase inhibitor. Moreover, they talk about the species of proteinases present in lysosomes and are thought to degrade various species of cellular proteins.