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1.
Natl J Maxillofac Surg ; 15(1): 121-130, 2024.
Article in English | MEDLINE | ID: mdl-38690245

ABSTRACT

Introduction: Conventional implants are associated with ridge augmentation/sinus lift procedures in vertically insufficient ridges, which increase morbidity and healing time. Short implants provided some hope in this context. The present study considered the use of ultra-short implants in vertically insufficient posterior mandibular ridges and evaluated their success. Hence, study was done to evaluate the success of ultra-short implants in partially edentulous posterior mandible clinically and radiographically. Materials and Methods: The study is a "Naïve direct comparison" of ultra-short implants to conventional implants for assessing their success in vertically insufficient posterior mandibular ridges. A total of 10 ultra-short implants were placed in a partially edentulous posterior mandibular ridge with at least 8-mm horizontal (at crest) and vertical dimensions. A delayed loading was done at three-month follow-up. Data acquisition was done at baseline (immediately after loading), 6-, 9-, 12-month intervals. Parameters assessed were marginal bone loss (MBL), probing pocket depth reduction (PPDR), modified plaque index (mPI), modified gingival index (mGI). Results: All the placed 10 implants survived, and no failure was observed. "Independent sample t-test" and "paired sample t-test" was done for intergroup and intragroup analysis, respectively. Intergroup comparison between the ultra-short and conventional implants presented a statistically insignificant difference between all the parameters at all the follow-up visits (baseline, 6-, 9-, 12 months). Conclusions: Within the limitations, it was thus concluded that ultra-short implants may be considered as a viable treatment option for vertically insufficient mandibular ridge. Further, long-term randomized controlled trials are required to establish the evidence.

2.
Int J Periodontics Restorative Dent ; (7): s264-s282, 2023 Oct 24.
Article in English | MEDLINE | ID: mdl-37879062

ABSTRACT

Periodontal intrabony defects (IBDs) are commonly encountered in dental practice and are usually treated by open flap debridement (OFD) with or without bone grafts and/or guided tissue regeneration (GTR), platelet-rich fibrin (PRF), or other additives. A difficulty with these approaches is maintaining the space for bone growth at the determined location. In this report, autologous sticky bone (ASB) was used and compared to a simple mixture of PRF and bone graft (PRF-BG) using the identical graft material-bioactive glass morsels-to assess its regenerative potential in IBDs, as sticky bone is known to maintain the space, according to previous research. A total of 21 IBDs were treated by OFD, PRF-BG mixture, or ASB. Regenerative assessment was clinically and radiographically performed by CBCT at 1 year. All the treatment modalities (OFD, PRF-BG, and ASB) showed statistically significant improvements clinically and radiographically at 1 year in terms of probing pocket depth reduction (PPDR), clinical attachment level gain (CALG), CBCT defect fill (CBCT-DF), and CBCT defect resolution (CBCT-DR); P < .05. The ASB group depicted the most favorable results (P < .05) in terms of the parameters at 1 year followed by the PRF-BG group and then the OFD group. Treatment of periodontal IBDs with ASB resulted in significant improvements in clinical and CBCT parameters compared to baseline at 1 year, and intrasurgical graft handling was much better in the ASB group.


Subject(s)
Alveolar Bone Loss , Platelet-Rich Fibrin , Spiral Cone-Beam Computed Tomography , Humans , Alveolar Bone Loss/diagnostic imaging , Alveolar Bone Loss/surgery , Guided Tissue Regeneration, Periodontal/methods , Surgical Flaps/surgery , Periodontal Attachment Loss/surgery
3.
J Oral Biosci ; 61(2): 129-133, 2019 06.
Article in English | MEDLINE | ID: mdl-31235029

ABSTRACT

BACKGROUND: Glucose-6-phosphate dehydrogenase (G6PD) deficiency is an erythrocyte enzyme defect that amplifies the susceptibility of erythrocytes to oxidative stress due to excessive levels of reactive oxygen species. Consequently, erythrocyte destruction and hemolysis occur. HIGHLIGHT: The possible mechanism of oxidative stress-mediated destruction of erythrocytes in G6PD deficient individuals induced by periodontal infection is highlighted. CONCLUSION: Periodontal diseases feature systemic loading of reactive oxygen species, and they may increase the risk of hemolysis in individuals with G6PD deficiency.


Subject(s)
Glucosephosphate Dehydrogenase Deficiency , Periodontal Diseases , Erythrocytes , Glucosephosphate Dehydrogenase , Hemolysis , Humans
4.
J Esthet Restor Dent ; 27(6): 355-66, 2015.
Article in English | MEDLINE | ID: mdl-25988979

ABSTRACT

PURPOSE: Semilunar coronally advanced flap (SCAF) and its modifications or adjuncts have been proposed in the literature for root coverage. Low level laser therapy (LLLT) has been shown to enhance wound healing. The aim of this split-mouth randomized controlled clinical trial was to assess the effects of LLLT application with respect to root coverage after SCAF procedure for the treatment of human maxillary multiple adjacent facial gingival recessions. MATERIALS AND METHODS: Ten subjects with bilateral multiple adjacent maxillary facial gingival recession defects (Miller I and II) were included in this study (20 in test, 20 in control group). A diode laser (810 nm) at 0.3 watts was applied to test sites during and 1 week after surgery for 10 seconds. Comparisons of the surgical sites were made with clinical measurements. RESULTS: Statistically significant differences were observed between test and control sites in the change in gingival recession depth, gingival recession width, clinical attachment level, and width of the keratinized tissue measurements after 6 months (p = 0.003, p = 0.001, p = 0.006, and p =< 0.001, respectively). The test group presented significantly greater complete root coverage (N = 18/20, 90%) compared with the control group (N = 6/20, 30%) at 6 months post-operatively. CONCLUSION: Within the confines of this study, the results depicted that a Low Level Laser Technique application may enhance the predictability of SCAF procedure. Further long-term studies with more sample sizes are needed for a stronger evidence base. CLINICAL SIGNIFICANCE: Gingival recessions are commonly encountered in dentistry and pose an esthetic concern. Minimal gingival recessions can be treated by a Semilunar Coronally Advanced Flap (SCAF), but the predictability and stability of the outcomes are quiet questionable. In the present report, a Low Level Laser Technique (LLLT) application adjunct to SCAF depicted a significant improvement in the predictability and stability of root coverage outcomes (for a period of 6 months) compared with as achieved by SCAF alone. From this report, it can be stated that LLLT may be effectively used in a day to day practice for enhancing the root coverage outcomes of SCAF.


Subject(s)
Gingival Recession/surgery , Low-Level Light Therapy , Maxilla/surgery , Humans
5.
Food Chem ; 142: 430-8, 2014 Jan 01.
Article in English | MEDLINE | ID: mdl-24001862

ABSTRACT

Cicer α-galactosidase was immobilized onto functionalized graphene with immobilization efficiency of 84% using response surface methodology (Box-Behnken design). The immobilized enzyme had higher thermal stability than the soluble one, attractive for industrial applications. Immobilization of the enzyme lowered the Km to 1/3rd compared to the soluble enzyme. Raffinose family oligosaccharides (RFOs) are mainly responsible for flatulence by taking soybean derived food products. The immobilized enzyme can be used effectively for the hydrolysis of RFOs. After ten successive runs, the immobilized enzyme still retained approximately 60% activity, with soybean RFOs. The easy availability of enzyme source, ease of its immobilization on matrices, non-toxicity, increased stability of immobilized enzyme and effective hydrolysis of RFOs increase the Cicer α-galactosidase application in food processing industries.


Subject(s)
Cicer/enzymology , Plant Proteins/chemistry , alpha-Galactosidase/chemistry , Enzyme Stability , Enzymes, Immobilized/chemistry , Graphite/chemistry , Hydrogen-Ion Concentration , Hydrolysis , Kinetics , Nanostructures/chemistry , Oligosaccharides/chemistry , Temperature
6.
Appl Biochem Biotechnol ; 169(8): 2315-25, 2013 Apr.
Article in English | MEDLINE | ID: mdl-23446984

ABSTRACT

Physiologically as well as industrially, α-galactosidases are very important enzymes, but very little is known about the stability and folding aspect of enzyme. In the present study, we have investigated the temperature, pH, and guanidine hydrochloride (GuHCl) induced unfolding of Cicer α-galactosidase using circular dichroism and fluorescence spectroscopy. Strong negative ellipticities at 208, 215, and 222 nm indicate the presence of both α and ß structures in Cicer α-galactosidase and showed that its secondary structure belongs to α + ß class of proteins with 31 % α-helicity. For Cicer α-galactosidase the emission maximum was found to be 345 nm which suggests that tryptophan residues are less exposed to solvent. However, at pH 2.0, protein showed blue-shift. This state of protein lacked activity but it retained significant secondary structure. Enhanced binding of ANS at pH 2.0 indicated significant unfolding and exposure of hydrophobic regions. The unfolded state of Cicer α-galactosidase showed a red-shift of 15 nm with a concomitant decrease in the fluorescence intensity. The enzyme maintained its native structure and full activity up to 40 °C; however, above this temperature, denaturation was observed.


Subject(s)
Cicer/enzymology , Guanidine/pharmacology , alpha-Galactosidase/chemistry , Circular Dichroism , Hydrogen-Ion Concentration , Protein Structure, Secondary , Spectrometry, Fluorescence , Temperature , alpha-Galactosidase/metabolism
7.
Carbohydr Res ; 358: 61-6, 2012 Sep 01.
Article in English | MEDLINE | ID: mdl-22818828

ABSTRACT

Cicer α-galactosidase was immobilized onto chitosan and Amberlite with immobilization efficiency of 62% and 51%, respectively. Compared to soluble enzyme, immobilized enzyme had a broader operational pH range and thermal stability. Temperature optimum for chitosan immobilized enzyme and Amberlite immobilized enzyme was 70°C, whereas it was 50°C for soluble enzyme. After 120days storage at 4°C chitosan immobilized enzyme retained 54% activity and Amberlite immobilized enzyme showed 32% activity. After using the immobilized enzymes 12 times, chitosan immobilized enzyme showed 52% activity, while Amberlite immobilized enzyme retained 22% activity with pNPGal. The immobilized enzyme exhibited higher K(m) compared to the soluble enzyme. Raffinose family oligosaccharides (RFOs) are mainly responsible for flatulence on taking of soybean derived food products. Immobilized enzyme can be used effectively for the hydrolysis of RFOs. After five runs, chitosan and Amberlite immobilized enzyme retained 53% and 34% activity, respectively with soybean RFOs. The easy availability of enzyme source, ease of its immobilization on matrices, non-toxicity and low cost of matrices, increased stability of immobilized enzyme, and effective hydrolysis of RFOs makes it a suitable product with potential applications at industries.


Subject(s)
Chitosan/chemistry , Cicer/enzymology , Enzymes, Immobilized/chemistry , Enzymes, Immobilized/metabolism , Resins, Synthetic/chemistry , alpha-Galactosidase/chemistry , alpha-Galactosidase/metabolism , Oligosaccharides/chemistry , Oligosaccharides/metabolism , Raffinose/chemistry
8.
J Agric Food Chem ; 60(12): 3253-9, 2012 Mar 28.
Article in English | MEDLINE | ID: mdl-22385353

ABSTRACT

Glycosylated α-galactosidase (melibiase) has been purified from white chickpea ( Cicer arietinum ) to 340-fold with a specific activity of 61 units/mg. Cicer α-galactosidase showed a M(r) of 45 kDa on SDS-PAGE and by MALDI-TOF. The optimum pH and temperature with pNPGal were 4.5 and 50 °C, respectively. The K(m) for hydrolysis of pNPGal was 0.70 mM. Besides hydrolyzing the pNPGal, Cicer α-galactosidase also hydrolyzed natural substrates such as melibiose, raffinose, and stachyose very effectively; hence, it can be exploited commercially for improving the nutritional value of soy milk. Galactose was found to be a competitive inhibitor. The property of this enzyme to cleave the terminal galactose residues can be utilized for converting the group B erythrocytes to group O erythrocytes.


Subject(s)
Cicer/enzymology , Seeds/enzymology , alpha-Galactosidase/isolation & purification , alpha-Galactosidase/metabolism , Blood Group Antigens/metabolism , Hydrogen-Ion Concentration , Kinetics , Metals/pharmacology , Oligosaccharides/metabolism , Raffinose/chemistry , Substrate Specificity , Temperature
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