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Incorporation of Phosphoproteins and Phenol-Bound Proteins Into the Cuticle of Periplaneta Americana

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Incorporation of Phosphoproteins and Phenol-Bound Proteins Into the Cuticle of Periplaneta Americana Virginia Commonwealth University VCU Scholars Compass Theses and Dissertations Graduate School 1976 Incorporation of Phosphoproteins and Phenol-Bound Proteins into the Cuticle of Periplaneta americana Joseph Atchison Florence IV Follow this and additional works at: https://scholarscompass.vcu.edu/etd Part of the Biology Commons © The Author Downloaded from https://scholarscompass.vcu.edu/etd/4554 This Thesis is brought to you for free and open access by the Graduate School at VCU Scholars Compass. It has been accepted for inclusion in Theses and Dissertations by an authorized administrator of VCU Scholars Compass. For more information, please contact [email protected]. School of Arts and Sciences Virginia Commonwealth University This is to certify that the thesis prepared by Joseph Atchison Florence IV entitled Incorporation of phosph::>proteins and phenol-bound proteins into the cuticle of Periplaneta americana has been approved by his committee as satisfactory completion of the thesis requirement for the Master of Science degree in Biology. Di.rector of Thesis VYr!!inia Commonwealtfr Incorporation of Phosphoproteins and Phenol-bound Proteins into the Cuticle of Periplaneta americana A thesis submitted in partial fulfillment of the requirements for the degree of Master of Science at Virginia Commonwealth University THESIS by Joseph Atchison Florence IV Directors Dr. Richard R, Mills frofessor of Biology Virginia Commonwealth University Richmond, Virginia August, 1976 ii DEDICATION This thesis is dedicated to the ubiquitous cockroach. May he rest in peace. iii ACKNOWLEDGEMENTS My deepest regards and sincerest appreciation are expressed to Ms. Mary Lou Strickland without whom I would have not completed this work. Her assistance has been invaluable. I would also like to express thanks to Dr. Richard R. Mills, mentor and entomologist par excellence. His ability to communicate his knowledge and share his enthusiasm for living and accomplishing my goals in life have made working with him an experience to remember. My thanks are also expressed to my professors and the professors of the department who have helped me accomplish my work. My compatriots of biology are also to be remembered: John Clore, Ellen Thomen, Nancy Taylor, John Krolak, Danny Custer, Mark Welsh, Greg Brown, and all the other graduate students that have shared their knowledge and experiences with me. Without these friends this work could never have been accomplished. iv TABLE OF OONTENTS Page LIST OF TAm..ES.. .. .• . .. • .. .• .• • . .• • .. .. • . .• . .. .• • .. .. • • . vi LIST OF F"IGURES.••..•••.••••.• ,••••..•••..••••.••••..•.•.••• . vii ABSTRACT.... •. • •• •• •• . • • •• •. • . .. •• .• .• . •. .• . .. •. • . •. .. •• . • X INTIDDUCTION. • • • . • . • • . • . • • . • . • • • . • • • • • . • . • . • . • . • • • • • • • • • . • . 1 OBJECTIVES.• .• . .• • . •. • • . .• .• • •• • • • .. .• .• .. • . • . • .• .• • • •• • . • • . 3 LITERATURE REVIEW••••••••••••• , •••• ,......................... 4 The Sclerotization Process in Cuticle Fonnation............................................... 4 Enzymes Involved in the Synthesis of Sclerotization Agent •••••••••••••.•••••••••••••••••••••. 27 Hormonal Control of Moulting and Tanning ••••••••••.•.••. 36 EXPERIMEl'rT.AI.s••••••••••••••• , •• ,• •• • • •• • • • •• • • • •• • • •• •• •• • •• •• l+8 METIDDS AND MATERIALS•••••••••••••••••••••••••••• , •• • •• •• • • •• 49 Phosphate Incorporation into Proteins and Cuticle. .. .. .. .. .. .. .. .. .. .. .. .. .. .. .. .. .. .. 49 llipamine Metabolites Binding to Cuticle Proteins.. .. .. .. .. .. .. .. .. .. .. .. .. .. .. .. .. .. .. 60 In Vitro Binding of NADA to Lysyl-lysine •••••••••••••••• 62 RESlJI,TS • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • 6 5 Phosphate Incorporation into Proteins and Cuticle .........................· ........................ 65 llipamine Metabolites Binding to Cuticle Proteins. .. .. .. .. .. .. .. .. .. .. .. .. .. .. .. 99 In Vitro Binding of NADA to Lysyl-lysine •••••••••••••••. 108 DISCUSSION..• • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • • 142 Phosphate Incorporation into Proteins and Cuticle ................................................. 142 llipamine Metabolites Binding to Cuticle Proteins................................................ 1� V Page In Vitro Binding 0£ NADA to Lysyl-lysine •••••••••••.•.•• 146 REF'ERmilCES.• •• • •• • •• • •. • •• • •• • • • •• • • •• •• • . • • •• • . •• .• • • •• • . •• • 1 l.J8 APP�X •••••.••.•.....•••.•.•.•..••.••.••... ·.. •. .• • .• • • . 18 5 VITA••• ......••...•... � ..•......•......•.•.•........•.. c • • • • • 187 vi LIST OF TABLES Table Page 3 1, Computer Program of Zp Activity••••••••••••••••••••••••• .50 2. Statistical Analysis System P:rogram of Phosphate Incorporation••••••••••••••.••••.••••••••••••.. 53 3, Least Squares Standard Curve Program.•••••••.•••••••••••• 57 4. Rf Values of Metabolites of Phosphate Metabolism.•.•••••. 70 5, Incorporation of Labelled :ro4 and Phosphop:rote;i.ns into the Cockroach Cuticle•••••••••••••..••••••••••••.••. 97 6. Rf Values f:rom fupamine Metaboliles when Incubated with Cuticle P:rotein.•••.•...••.•..••.••••••••.••.•.••••• 104 7, Rf Values of Possible fupamine Metabolites f:rom Various Literature Sources.• •• • • .• .• • • • •. •• • • • .• • • • • •• •• . 106 vii LIST OF FIGURES Figure Page 1. Sequence of Products Between Quinones and Proteins................ � ................... ·. .. .. .. 7 2. Proposed Mechanism of Sclerotization Prior to 1974....... 10 J. Modified Scheme of Cuticle Sclerotization••••.••.•. •••.•• 12 4. Andersen's Proposal for Sidechain Sclerotization......... 15 5. Dia.grammatic Representation of a Section of Mature Cuticle and Epidermis....• • • •• • • . • • •• • • •• • • • •• •• . • •• •• . •. 17 6. Representation of Changes in the Integu.�ent During Ecdysis................... ........................ ,...... 20 7. Structures of Hyd:rolysates of Possible Sclerotization Agents .••••.•••.• ,....................................... 24 8. P�thway of Sclerotization Agent ...••••.•••••••..•••••..•. 32 9. Mechanism of Binding of the Sclerotization Agent .•....•.• 34 10. Structure of Ecdysone.••••.•.•..••••.••••••••••••••••••.. 37 11. Two Pathways of Tyrosine Metabolism•••..•••••••••.•...... 41 12. Action of Bursicon on the Haemocyte ..••••••••••••.•••••.. 46 13. Representative Chromatograms of Phosphate Metabolites from the Haemolymph in 2, 4 and 24 hour Incubations. .. .. .. .. .. .. .. .. .. .. .. .. .. .. .. 66 14. Representative Electropherograms of Phospt>.ate Metabo.lites from Haemolymph.. •• • •• • • •• • •• •• . •• . •• • .. .. •• • 68 15. Two Hour P-JO Gel Chromatograph (1st experiment)•..•.•.•• 72 16. Two Hour P-JO Gel Chromatograph (2nd experiment).••.••.•. 74 17. Two Hour P-JO Gel Chromatograph (3rd experiment) .••••...• 76 18. Two Hour P-JO Gel Chromatograph (composite).••.••••.••••• 78 viii Figure Page 19. Four Hour P-30 Gel Chromatograph (1st experiment)••.•••.. 80 20. Four Hour P-30 Gel Chromatograph (2nd experiment)........ 82 21. Four Hour P-30 Gel Chromatograph (3rd experiment)........ 84 22. Four Hour P-30 Gel Chromatograph (composite)............. 86 23. Twenty-four Hour P-30 Gel Chromatograph (1st experiment). 88 24. Twenty-four Hour P-30 Gel Chromatograph (2nd experiment). 90 25. Twenty-four Hour·P-30 Gel Chromatograph (3rd experiment). 92 26. Twenty-four Hour P-30 Gel Chromatograph (composite)...... 94 27. Representative Radiochromatograms of llipamine Metabolite Binding Experiment� with Cuticle Soluble Proteins.. .. .. .. .. .. .. .. .. .. .. .. .. .. .. .. 100 28. Representative Radiochromatograms of llipamine Metabolite Binding Experiments with Cuticle lfomogenate . ..............•.............•................. 102 29. Elution -Profile. of Non-labelled N-acetyldopamine, lysyl-lysine and cuticle homogenate...••••.••••••.••••.•• 109 30. Duplicate Elution Profile.•••..••••••.•.••.•••••.••.•••.• 111 31. Elution Profile or14c-N-acetyldopamine, Lysyl-lysine and Cuticle Homogenate (ninhydrin and UV)•••••••••••••••• 113 32. Elution Profile of 14c-N-acetyldopamine, Lysyl-lysine and Cuticle Homogenate (cpm and UV)•••••••••••••••••••••• 115 33. Radiochromatograms of Column Eluant 14c-N-acetyldopamine Lysyl-lysine and Cuticle Homogenate.••••••••••••••••••••• 117, 34. Electropherograms of Column E,l:uant 14c-N-a.cetyldopamine Lysyl-lysine and Cuticle Homogenate•••••••••••.•••••••••• 119 35. Graph of Eluant from P-2 Gel Colllinn on N-acetyldopamine and Lysyl-lysine metabolites (ninhydrin and OD)•••••••.••. 122 36. Chromatograms and Electropherograms of Incubant of N-acetyldopamine and Lysyl-lysine•••••••••.••••••••.•••.• 124 37. Representative UV Spectra of the Oxidized Product of N-acetyldopamine........... .......•................... 126 38. NMR of Fraction A and B from N-acetyldopamine- Lysyl-lysine Binding••••••••.•••••.• •.•••••.•••••••••••.• 128 ix.:. Figure Page Dz°, 39. NMR of N-acet!ldopamine in DMS and lysyl-lysine in n2o ..................................... 131 40. NMR of possible metabolites of the sclerotization agent and di peptides ..................................· .. 135 .x Incorporation of Phosphoproteins and Phenol-bound Proteins into the Cuticle of Periplaneta americana ABSTRACT A thesis submitted in partial fulfillment of the requirements for the degree of Master of Science at Virginia Commonwealth University by Joseph Atchison Florence IV Director: Dr. Richard R. Mills Professor of
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